B. Matthews

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Comparison of the predicted and observed secondary structure of T4 phage lysozyme.

B. Matthews, 1975, Biochimica et biophysica acta.

Substantial increase of protein stability by multiple disulphide bonds

B. Matthews, M. Matsumura, G. Signor, 1989, Nature.

Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.

U. Sauer, B. Matthews, D. P. Sun, 1991, Biochemistry.

Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme.

B. Matthews, S. Dao-pin, D. E. Anderson, 1991, Biochemistry.

A mutant T4 lysozyme displays five different crystal conformations

B. Matthews, H. R. Faber, Brian W. Matthews, 1990, Nature.

Structural studies of mutants of T4 lysozyme that alter hydrophobic stabilization.

B. Matthews, M. Matsumura, D. P. Sun, 1990, The Journal of biological chemistry.

Energetic origins of specificity of ligand binding in an interior nonpolar cavity of T4 lysozyme.

B. Matthews, W. Baase, A. Morton, 1995, Biochemistry.

A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene

B. Matthews, W. Baase, J. A. Wozniak, 1993, Nature.

A model binding site for testing scoring functions in molecular docking.

B. Matthews, B. Shoichet, W. Baase, 2002, Journal of molecular biology.

Docking molecules by families to increase the diversity of hits in database screens: Computational strategy and experimental evaluation

B. Matthews, B. Shoichet, W. Baase, 2001, Proteins.

The extension of the isomorphous replacement method to include anomalous scattering measurements

B. Matthews, 1966 .

From the new Editor

B. Matthews, 2007 .

Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.

B. Matthews, J. A. Wozniak, X. Zhang, 1995, Journal of molecular biology.

Binding of small electron-dense ligands in large protein cavities

B. Matthews, W. Baase, Michael L. Quillin, 1996 .

An efficient general-purpose least-squares refinement program for macromolecular structures

Brian W. Matthews, B. Matthews, D. Tronrud, 1987 .

Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.

B. Matthews, K. Wilson, L. Shewchuk, 1992, Proceedings of the National Academy of Sciences of the United States of America.

The response of T4 lysozyme to large‐to‐small substitutions within the core and its relation to the hydrophobic effect

B. Matthews, W. Baase, J. Xu, 1998, Protein science : a publication of the Protein Society.

Solvent content of protein crystals.

B. Matthews, 1968, Journal of molecular biology.

Structural and genetic analysis of protein stability.

B. Matthews, B W Matthews, 1993, Annual review of biochemistry.

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.

B. Matthews, H. Nicholson, W. Becktel, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3

Brian W. Matthews, B. Matthews, M. Matsumura, 1988, Nature.

Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme.

B. Matthews, H. Nicholson, S. Dao-pin, 1991, Biochemistry.

Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.

J A Wozniak, B. Matthews, W. Baase, 1991 .

Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme.

B. Matthews, J. Hurley, W. Baase, 1993, Journal of molecular biology.

Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions.

U. Sauer, B. Matthews, D. San, 1991, The Journal of biological chemistry.

Multiple alanine replacements within α‐helix 126–134 of T4 lysozyme have independent, additive effects on both structure and stability

B. Matthews, W. Baase, X. Zhang, 1991, Protein science : a publication of the Protein Society.

Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect.

B. Matthews, W. Baase, A. Eriksson, 1992, Science.

Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59

Uwe Sauer, Brian W. Matthews, U. Sauer, 1993 .

Enhanced protein thermostability from designed mutations that interact with α-helix dipoles

B. Matthews, H. Nicholson, W. Becktel, 1990, Nature.

The conformation of thermolysin.

B. Matthews, L. Weaver, W. R. Kester, 1974, The Journal of biological chemistry.

Structural analysis of zinc substitutions in the active site of thermolysin

D. R. Holland, B. Matthews, A. Hausrath, 1995, Protein science : a publication of the Protein Society.

Structure of thermolysin refined at 1.6 A resolution.

B. Matthews, M. Holmes, B W Matthews, 1982, Journal of molecular biology.

A relationship between protein stability and protein function.

B K Shoichet, B. Matthews, B. Shoichet, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Chlorophyll arrangement in a bacteriochlorophyll protein from Chlorobium limicola

B. Matthews, R. Fenna, B. W. Matthews, 1975, Nature.

Structure of a bacteriochlorophyll a-protein from the green photosynthetic bacterium Prosthecochloris aestuarii.

B. Matthews, M. Bolognesi, J. Olson, 1979, Journal of molecular biology.

Refinement of the Structure of a Water-Soluble Antenna Complex from Green Photosynthetic Bacteria by Incorporation of the Chemically Determined Amino Acid Sequence

B. Matthews, D. Tronrud, 1993 .

Cryo-cooling inmacromolecular crystallography : advantages , disadvantages andoptimization

B. Matthews, D. Juers, 2004 .

Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin.

D E Tronrud, B. Matthews, D. Tronrud, 1989, European journal of biochemistry.

The role of solvent transport in cryo-annealing of macromolecular crystals.

B. Matthews, D. Juers, 2004, Acta crystallographica. Section D, Biological crystallography.

Three-dimensional structure of β-galactosidase from E. coli.

B. Matthews, R. Dubose, R. Jacobson, 1994, Nature.

Accurate calculation of the density of proteins.

B. Matthews, Michael L. Quillin, 2000, Acta crystallographica. Section D, Biological crystallography.

Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution.

B. Matthews, L. Weaver, 1987, Journal of molecular biology.

The γ Turn. Evidence for a New Folded Conformation in Proteins

B. Matthews, 1972 .

The three dimensional structure of the lysozyme from bacteriophage T4.

B. Matthews, S. Remington, 1974, Proceedings of the National Academy of Sciences of the United States of America.

Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme.

B. Matthews, B. Mooers, 2006, Acta crystallographica. Section D, Biological crystallography.

Crystallographic data for sturgeon holo-D-glyceraldehyde-3-phosphate dehydrogenase: a holo-D-glyceraldehyde-3-phosphate dehydrogenase with crystallographic 2-fold symmetry.

B. Matthews, S. Remington, M. Holmes, 1977, Journal of molecular biology.

Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.

B. Matthews, K. Wilson, B. Malcolm, 1993, The Journal of biological chemistry.

Lessons from the lysozyme of phage T4

Dale E Tronrud, Brian W Matthews, B. Matthews, 2010, Protein science : a publication of the Protein Society.

Structure-Based Design of an Inhibitor of the Zinc Peptidase Thermolysin

Paul A. Bartlett, Brian W. Matthews, Bradley P. Morgan, 1994 .

Testing a flexible-receptor docking algorithm in a model binding site.

Brian K Shoichet, Brian W Matthews, B. Matthews, 2004, Journal of molecular biology.

Structural basis of amino acid alpha helix propensity.

B. Matthews, M. Blaber, X. Zhang, 1993, Science.

Control of enzyme activity by an engineered disulfide bond.

B. Matthews, M. Matsumura, B W Matthews, 1994, Science.

Stabilization of functional proteins by introduction of multiple disulfide bonds.

B. Matthews, M. Matsumura, B W Matthews, 1991, Methods in enzymology.

The helix-turn-helix DNA binding motif.

B. Matthews, R. Brennan, B W Matthews, 1989, The Journal of biological chemistry.

Genetic and structural analysis of the protein stability problem.

B. Matthews, B W Matthews, Brian W. Matthews, 1987, Biochemistry.

Core-packing constraints, hydrophobicity and protein design.

B. Matthews, E. Baldwin, B W Matthews, 1994, Current opinion in biotechnology.

[1] Recent transformations in structural biology.

Brian W Matthews, B. Matthews, 1997, Methods in enzymology.

A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis.

Brian W Matthews, B. Matthews, W. Baase, 1995, Biophysical chemistry.

Structural features of the g subunit of the Escherichia coli F 1 ATPase revealed by a 4.4-Å resolution map obtained by x-ray crystallography

B. Matthews, A. Hausrath, G. Grüber, 1999 .

Sorting the chaff from the wheat at the PDB

Dale E Tronrud, Brian W Matthews, B. Matthews, 2008, Protein science : a publication of the Protein Society.

Structure of the cro repressor from bacteriophage λ and its interaction with DNA

B. Matthews, D. Ohlendorf, W. Anderson, 1981, Nature.

Comparison of protein structures.

M G Rossmann, B. Matthews, M. Rossmann, 1985, Methods in enzymology.

David Davies: Structural biologist and mentor

B. Matthews, 2017, Protein science : a publication of the Protein Society.

A test of proposed rules for helix capping: Implications for protein design

B. Matthews, W. Baase, M. Sagermann, 2002, Protein science : a publication of the Protein Society.

The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue.

B. Matthews, L. Weaver, M. Grütter, 1995, Journal of molecular biology.

Structure of Escherichia coli exonuclease I suggests how processivity is achieved

B. Matthews, W. A. Breyer, 2000, Nature Structural Biology.

Hydrophobic core repacking and aromatic–aromatic interaction in the thermostable mutant of T4 lysozyme ser 117 → phe

D. E. Anderson, B. Matthews, J. Hurley, 1993, Protein science : a publication of the Protein Society.

B. Matthews, W. Baase, A. Eriksson, 1993, Journal of molecular biology.

Conservation of solvent‐binding sites in 10 crystal forms of T4 lysozyme

B. Matthews, X. Zhang, B W Matthews, 1994, Protein science : a publication of the Protein Society.

Local scaling: a method to reduce systematic errors in isomorphous replacement and anomalous scattering measurements

E. W. Czerwinski, B. Matthews, 1975 .

The structure of thermolysin: an electron density map at 2-3 A resolution.

B. Matthews, P. Colman, J. Jansonius, 1972, Journal of molecular biology.

Nerve growth factor in different crystal forms displays structural flexibility and reveals zinc binding sites.

D. R. Holland, B. Matthews, L. Cousens, 1994, Journal of molecular biology.

Substitution with selenomethionine can enhance the stability of methionine-rich proteins.

B. Matthews, W. Baase, A. Hausrath, 1999, Journal of molecular biology.

Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.

B. Matthews, M. Blaber, D. Heinz, 1993, Biochemistry.

An evaluation of electron micrographs of bacteriochlorophyll a-protein crystals in terms of the structure determined by x-ray crystallography.

B. Matthews, S. Remington, R. Fenna, 1977, Journal of ultrastructure research.

Use of experimental crystallographic phases to examine the hydration of polar and nonpolar cavities in T4 lysozyme

B. Matthews, Michael L. Quillin, Lijun Liu, 2008, Proceedings of the National Academy of Sciences.

Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive.

B K Shoichet, B. Matthews, B. Shoichet, 1995, Protein engineering.

Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases.

B. Matthews, A. Monzingo, B W Matthews, 1984, Biochemistry.

Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond.

H M Holden, D E Tronrud, B. Matthews, 1987, Science.

Crystal structure of the BstDEAD N-terminal domain: a novel DEAD protein from Bacillus stearothermophilus.

B. Matthews, A. B. Carmel, 2004, RNA.

High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer.

B. Matthews, M. Mossing, R. Albright, 1996, Biochemistry.

Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide.

Brian W Matthews, Edwin M Westbrook, B. Matthews, 2004, Journal of molecular biology.

Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme.

B. Matthews, S. Roderick, 1993, Biochemistry.

The structure of rat mast cell protease II at 1.9-A resolution.

Hans Neurath, Brian W. Matthews, Richard G. Woodbury, 1984, Biochemistry.

Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme

B. Matthews, W. Baase, Michael L. Quillin, 2001, Protein science : a publication of the Protein Society.

STRAT: a program to optimize X-ray data collection on an area detector system

B. Matthews, X.-J. Zhang, X.‐J. Zhang, 1993 .

Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.

B. Matthews, W. Baase, F. Dahlquist, 1999, Biochemistry.

Sequential reorganization of β‐sheet topology by insertion of a single strand

B. Matthews, W. Baase, M. Sagermann, 2006 .

Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability.

B. Matthews, W. Baase, L. Weaver, 2003, Biophysical chemistry.

Metalloaminopeptidases: common functional themes in disparate structural surroundings.

B. Matthews, W. Lowther, 2002, Chemical reviews.

Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.

B. Matthews, L. Weaver, J. Bazan, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Protein Structure Initiative: getting into gear

B. Matthews, 2007, Nature Structural &Molecular Biology.

Structure of the DNA binding region of prospero reveals a novel homeo-prospero domain.

B. Matthews, C. Doe, J. Ryter, 2002, Structure.

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.

B. Matthews, H. Nicholson, W. Becktel, 1990, Proceedings of the National Academy of Sciences of the United States of America.

How Cro and lambda-repressor distinguish between operators: the structural basis underlying a genetic switch.

B. Matthews, R. Albright, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Thermolysin in the absence of substrate has an open conformation.

B. Matthews, A. Hausrath, 2002, Acta crystallographica. Section D, Biological crystallography.

Structure-based design of a lysozyme with altered catalytic activity

B. Matthews, L. Weaver, R. Kuroki, 1995, Nature Structural Biology.

Changes to crystals of Escherichia coli beta-galactosidase during room-temperature/low-temperature cycling and their relation to cryo-annealing.

B. Matthews, G. Borgstahl, H. Bellamy, 2007, Acta crystallographica. Section D, Biological crystallography.

Cro repressor protein and its interaction with DNA.

B. Matthews, D. Ohlendorf, W. Anderson, 1983, Cold Spring Harbor symposia on quantitative biology.

Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda.

B. Matthews, D. Ohlendorf, C. Pabo, 1989, Journal of molecular biology.

Use of site-directed mutagenesis to obtain isomorphous heavy-atom derivatives for protein crystallography: cysteine-containing mutants of phage T4 lysozyme.

B. Matthews, D. P. Sun, L. Weaver, 1987, Protein engineering.

Atomic coordinates for the chlorophyll core of a bacteriochlorophyll a-protein from green photosynthetic bacterial.

B. Matthews, L. F. Eyck, R. Fenna, 1977, Biochemical and biophysical research communications.

Structure of a bacteriochlorophyll-protein from the green photosynthetic bacterium Chlorobium limicola: crystallographic evidence for a trimer.

B. Matthews, J. Olson, R. Fenna, 1974, Journal of molecular biology.

Structure and symmetry of oligomeric enzymes.

B. Matthews, S. Bernhard, 1973, Annual review of biophysics and bioengineering.

A method of obtaining a stereochemically acceptable protein model which fits a set of atomic coordinates

B. Matthews, L. Weaver, L. F. Eyck, 1976 .

Direct and indirect roles of His‐418 in metal binding and in the activity of β‐galactosidase (E. coli)

R. E. Huber, B. Matthews, D. Juers, 2009, Protein science : a publication of the Protein Society.

Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase.

B. Matthews, N. Brot, H. Weissbach, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression

Jun O. Liu, B. Matthews, A. Addlagatta, 2006, Proceedings of the National Academy of Sciences.

Transformations in structural biology: a personal view.

B. Matthews, 2003, Methods in enzymology.

The Three Dimensional Structure of the Lysozyme from Bacteriophage T4 (protein

B. Matthews, 2022 .

Structure of the cro repressor from bacteriophage lambda and its interaction with DNA.

B. Matthews, D. Ohlendorf, W. Anderson, 1981, Nature.

A structural view of the action of Escherichia coli (lacZ) beta-galactosidase.

B. Matthews, S. Withers, J. McCarter, 2001, Biochemistry.

Symmetry, molecular weight and crystallographic data for sweet potato -amylase.

B. Matthews, P. Colman, 1971, Journal of molecular biology.

Purification, crystallization and preliminary X-ray analysis of the novel DEAD protein BstDEAD from Bacillus stearothermophilus.

B. Matthews, A. B. Carmel, 2003, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment.

B. Matthews, I. Korndörfer, J. Salerno, 2000, Acta crystallographica. Section D, Biological crystallography.

Crystallization of a complex of cro repressor with a 17 base-pair operator.

B. Matthews, R. Brennan, W. Anderson, 1986, Journal of molecular biology.

Determination of protein molecular weight, hydration, and packing from crystal density.

B. Matthews, 1985, Methods in enzymology.

Crystallographic data for complexes of the Cro repressor with DNA.

B. Matthews, D. Ohlendorf, W. Anderson, 1983, Journal of molecular biology.

Determination of molecular weight from protein crystals.

B. Matthews, Brian W. Matthews, 1974, Journal of molecular biology.

Some crystal forms of bovine chymotrypsinogen B and chymotrypsinogen A.

B. Matthews, 1968, Journal of molecular biology.

Toroidal structure of lambda-exonuclease.

B. Matthews, R. Kovall, 1998, Science.

Changes at Protein Science

B. Matthews, 2008 .

How amino-acid insertions are allowed in an α-helix of T4 lysozyme

Dirk W. Heinz, Brian W. Matthews, Frederick W. Dahlquist, 1993, Nature.

Relation between γ- and α-chymotrypsin

B. Matthews, G. Cohen, D. Davies, 1968 .

Proteins under pressure

B. Matthews, 2012, Proceedings of the National Academy of Sciences.

Structural basis of protein stability and DNA-protein interaction.

B. Matthews, 1985, Harvey lectures.

Inhibition of thermolysin and neutral endopeptidase 24.11 by a novel glutaramide derivative: X-ray structure determination of the thermolysin-inhibitor complex.

D. R. Holland, B. Matthews, K. James, 1994, Biochemistry.

The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis.

H M Holden, B. Matthews, H. Holden, 1989, The Journal of biological chemistry.

Structural basis of the action of thermolysin and related zinc peptidases

Brian W. Matthews, B. Matthews, 1988 .

Structure of crystalline -chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanism.

B. Matthews, R. Henderson, D. Blow, 1968, Journal of molecular biology.

Three-dimensional Structure of Tosyl-α-chymotrypsin

B. Matthews, R. Henderson, D. Blow, 1967, Nature.

The structure of E. coli β-galactosidase

B. Matthews, 2005 .

Three-dimensional structure of human basic fibroblast growth factor.

B. Matthews, A. Eriksson, L. Weaver, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin.

B. Matthews, S. Sieburth, D. Juers, 2005, Biochemistry.

Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis.

B. Matthews, W. Lowther, D. Rich, 1999, Biochemistry.

The crystal and molecular structure of the "metallic reflector" 1,5-bis(dimethylamino)pentamethinium perchlorate

B. Matthews, J. Selzer, 1976 .

Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases.

Jun O. Liu, B. Matthews, A. Addlagatta, 2006, Angewandte Chemie.

Binding of lanthanide ions to thermolysin.

B. Matthews, L. Weaver, 1974, Biochemistry.

How does cro repressor recognize its DNA target sites

B. Matthews, D. Ohlendorf, W. Anderson, 1983 .

Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues.

H M Holden, D E Tronrud, B. Matthews, 1989, Biochemistry.

A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substances.

B. Matthews, L. Weaver, W. R. Kester, 1977, Journal of molecular biology.

Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site

B. Matthews, L. Gay, A. Addlagatta, 2006, Proceedings of the National Academy of Sciences.

Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin.

B. Matthews, B. Roques, S. Roderick, 1989, Biochemistry.

Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis.

B. Matthews, M. Holmes, B W Matthews, 1982, Biochemistry.

Proposed α-helical super-secondary structure associated with protein-DNA recognition

B. Matthews, D. Ohlendorf, W. Anderson, 1982 .

Can small cyclic peptides have the activity and specificity of proteolytic enzymes?

B. Matthews, C. Craik, H. Neurath, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Toroidal Structure of λ-Exonuclease

B. Matthews, R. Kovall, 1997 .

Boron mimetics: 1,2-dihydro-1,2-azaborines bind inside a nonpolar cavity of T4 lysozyme.

B. Matthews, Shih‐Yuan Liu, Lijun Liu, 2009, Angewandte Chemie.

Structural basis for the unusual specificity of Escherichia coli aminopeptidase N.

B. Matthews, L. Gay, A. Addlagatta, 2008, Biochemistry.

The photochemistry of 3,5-disubstituted 1,4-dihydropyridines.

B. Matthews, J. Williams, U. Eisner, 1970, Tetrahedron.

A structural basis for processivity

B. Matthews, W. A. Breyer, 2001, Protein science : a publication of the Protein Society.

Escherichia coli repressor of biotin biosynthesis.

B. Matthews, D. Beckett, 1997, Methods in enzymology.

Structure and function of the methionine aminopeptidases.

B. Matthews, W. Lowther, 2000, Biochimica et biophysica acta.

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes.

R A Bradshaw, B. Matthews, S. Arfin, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Structural basis for the functional differences between type I and type II human methionine aminopeptidases.

Jun O. Liu, B. Matthews, A. Addlagatta, 2005, Biochemistry.

The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase.

B. Matthews, W. Lowther, A. Orville, 1998, Proceedings of the National Academy of Sciences of the United States of America.

The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution.

B. Matthews, I. Korndörfer, W. Fessner, 2000, Journal of molecular biology.

Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A.

B. Matthews, A. Hausrath, B W Matthews, 1994, The Journal of biological chemistry.

Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor.

D E Tronrud, B. Matthews, M. Holmes, 1983, Biochemistry.

LacZ β‐galactosidase: Structure and function of an enzyme of historical and molecular biological importance

R. E. Huber, B. Matthews, D. Juers, 2012, Protein science : a publication of the Protein Society.

Crystallization of β-galactosidase from Escherichia coli

B. Matthews, R. Jacobson, Raymond H. Jacobson, 1992 .

Structure and X-ray amino acid sequence of a bacteriochlorophyll A protein from Prosthecochloris aestuarii refined at 1.9 A resolution.

M F Schmid, D E Tronrud, B. Matthews, 1986, Journal of molecular biology.

Stabilization of phage T4 lysozyme by engineered disulfide bonds.

M Levitt, M. Levitt, B. Matthews, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Selling candles in a post-Edison world: phasing with noble gases bound within engineered sites.

B. Matthews, Michael L. Quillin, 2003, Acta crystallographica. Section D, Biological crystallography.

Generation of noble-gas binding sites for crystallographic phasing using site-directed mutagenesis.

B. Matthews, Michael L. Quillin, 2002, Acta crystallographica. Section D, Biological crystallography.

Crystal structure of lambda-Cro bound to a consensus operator at 3.0 A resolution.

B. Matthews, R. Albright, 1998, Journal of molecular biology.

Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex.

B. Matthews, R. Brennan, S. Roderick, 1990, Proceedings of the National Academy of Sciences of the United States of America.

DNA-binding proteins.

B. Matthews, D. Ohlendorf, W. Anderson, 1983, Science.

Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between β‐galactosidase and other glycohydrolases

R. E. Huber, B. Matthews, D. Juers, 2008, Protein science : a publication of the Protein Society.

Many gene-regulatory proteins appear to have a similar α-helical fold that binds DNA and evolved from a common precursor

B. Matthews, D. Ohlendorf, W. Anderson, 1983, Journal of Molecular Evolution.

A new DNA-binding motif in the Skn-1 binding domain–DNA complex

B. Matthews, P. Rupert, G. Daughdrill, 1998, Nature Structural Biology.

Common precursor of lysozymes of hen egg-white and bacteriophage T4

B. Matthews, S. Remington, M. Grütter, 1981, Nature.

An X-ray diffraction study of inhibited derivatives of α-chymotrypsin

B. Matthews, D. Blow, P. Sigler, 1966 .

Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3-->Pro.

B. Matthews, H. Nicholson, W. Baase, 1993, Journal of molecular biology.

Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function.

B. Matthews, Frantzy Etienne, N. Brot, 2002, Archives of biochemistry and biophysics.

Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing

Brian W. Matthews, Jack F. Kirsch, Allan C. Wilson, 1990, Nature.

Sequential reorganization of beta-sheet topology by insertion of a single strand.

B. Matthews, W. Baase, M. Sagermann, 2006, Protein science : a publication of the Protein Society.

Structural, functional, and evolutionary relationships between lambda-exonuclease and the type II restriction endonucleases.

B. Matthews, R. Kovall, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins.

B. Matthews, A. Barkan, G. J. Ostheimer, 2002, Structure.

Structural basis for the attachment of a paramyxoviral polymerase to its template.

Brian W Matthews, B. Matthews, F. Dahlquist, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme.

B. Matthews, W. Baase, J. Xu, 1996, Journal of molecular biology.

Second-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft.

B. Matthews, D. P. Sun, H. Nicholson, 1991, Biochemistry.

High resolution refinement of β‐galactosidase in a new crystal form reveals multiple metal‐binding sites and provides a structural basis for α‐complementation

R. E. Huber, B. Matthews, D. Wigley, 2000, Protein science : a publication of the Protein Society.

Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase

B. Matthews, A. Addlagatta, 2006, Protein science : a publication of the Protein Society.

The molecular basis of DNA–protein recognition inferred from the structure of cro repressor

B. Matthews, D. Ohlendorf, W. Anderson, 1982, Nature.

Kinetic studies on Cro repressor-operator DNA interaction.

B. Matthews, W. Anderson, J. Kim, 1987, Journal of molecular biology.

Comparison of the structures of Cro and λ repressor proteins from bacteriophage λ

B. Matthews, D. Ohlendorf, M. Lewis, 1983 .

An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides.

B. Matthews, A. Monzingo, D. Hangauer, 1984, Biochemistry.

Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis.

D. R. Holland, B. Matthews, K. Flaherty, 1992, Biochemistry.

Comparison of the structures of carboxypeptidase A and thermolysin.

B. Matthews, W. R. Kester, B W Matthews, 1977, The Journal of biological chemistry.

Three-dimensional structure of thermolysin.

B P Schoenborn, B. Matthews, B. Schoenborn, 1972, Nature: New biology.

The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB

Brian W. Matthews, B. Matthews, Frantzy Etienne, 2002, Nature Structural Biology.

Structure and thermal stability of phage T4 lysozyme.

B. Matthews, T. Alber, B W Matthews, 1987, Methods in enzymology.

The structure of E. coli beta-galactosidase.

B. Matthews, 2005, Comptes rendus biologies.

Crystallization of designed protein variants

B. Matthews, S. Dao-pin, H. R. Faber, 1990 .

Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution.

B. Matthews, D. Beckett, L. Weaver, 2006, Journal of molecular biology.

Structural basis of DNA-protein recognition.

B. Matthews, R. Brennan, 1989, Trends in biochemical sciences.

Structure of the DNA-binding region of lac repressor inferred from its homology with cro repressor.

B. Matthews, D. Ohlendorf, W. Anderson, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Structural Studies of DNA-Protein Interactions

B. Matthews, 1984 .

Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase.

R. E. Huber, B. Matthews, D. Juers, 2003, Biochemistry.

T. Steitz, B. Matthews, D. Ohlendorf, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Three-dimensional structure of beta-galactosidase from E. coli.

B. Matthews, R. Dubose, X. Zhang, 1994, Nature.

Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator

B. Matthews, D. Beckett, L. Weaver, 2001, Proceedings of the National Academy of Sciences of the United States of America.

High resolution structural studies of Cro repressor protein and implications for DNA recognition.

B. Matthews, D. Ohlendorf, W. Anderson, 1983, Journal of biomolecular structure & dynamics.

A STRUCTURAL ANALYSIS OF METAL SUBSTITUTIONS IN THERMOLYSIN

D. R. Holland, B. Matthews, A. Hausrath, 1995 .

Structural basis for the action of thermolysin.

B. Matthews, D. Tronrud, S. Roderick, 1992, Matrix (Stuttgart, Germany). Supplement.

Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?

B. Matthews, L. Weaver, M. Grütter, 1983, Nature.

Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution

N. Isaacs, B. Matthews, L. Weaver, 1985, Journal of Molecular Evolution.

The Bragg legacy: early days in macromolecular crystallography.

B. Matthews, 2013, Acta crystallographica. Section A, Foundations of crystallography.

Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity.

B. Matthews, M. Sagermann, 2002, Journal of molecular biology.

A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme.

B. Matthews, L. Weaver, R. Kuroki, 1993, Science.

X-ray crystallographic studies of the structure, function and evolution of proteins

B. Matthews, D. Ohlendorf, L. Weaver, 1982 .

Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: implications for the mechanism of catalysis.

B. Matthews, L. Weaver, S. Remington, 1981, Journal of molecular biology.

Relation between hen egg white lysozyme and bacteriophage T4 lysozyme: evolutionary implications.

S J Remington, B. Matthews, S. Remington, 1981, Journal of molecular biology.

Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile.

B. Matthews, L. Weaver, M. Grütter, 1987, Journal of molecular biology.

Multiple alanine replacements within a-helix 126-134 of T 4 lysozyme

B. Matthews, W. Baase, X.‐J. Zhang, 2002 .

11 – Bacteriochlorophyll-Proteins from Green Photosynthetic Bacteria*

B. Matthews, R. Fenna, 1979 .

Use of differentially substituted selenomethionine proteins in X-ray structure determination.

B. Matthews, N. Gassner, Brian W. Matthews, 1999, Acta crystallographica. Section D, Biological crystallography.

Parameter refinement in the multiple isomorphous‐replacement method

D. M. Blow, B. Matthews, D. Blow, 1973 .

Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme.

D E Tronrud, E Söderlind, B. Matthews, 1990, Journal of molecular biology.

Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae

Brian W. Matthews, Tom H. Stevens, B. Matthews, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Cloning, expression and crystallization of VMA13p, an essential subunit of the vacuolar H+-ATPase of Saccharomyces cerevisiae.

B. Matthews, M. Sagermann, 2000, Acta crystallographica. Section D, Biological crystallography.

Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme.

B. Matthews, N. Brot, H. Weissbach, 2000, Biochemistry.

Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme

B. Matthews, W. Baase, I. Vetter, 1996, Protein science : a publication of the Protein Society.

High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His.

J A Wozniak, B. Matthews, D. E. Anderson, 1989, Biochemistry.

Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.

J A Wozniak, B. Matthews, D. P. Sun, 1990, Science.

Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme

Tom Alber, Brian W. Matthews, B. Matthews, 1988, Nature.

Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme

Brian W Matthews, B. Matthews, W. Baase, 2009, Protein science : a publication of the Protein Society.

Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation.

Sol M Gruner, Brian W Matthews, B. Matthews, 2008, Biochemistry.

Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods.

B. Matthews, B. Mooers, 2004, Acta crystallographica. Section D, Biological crystallography.

Alanine‐scanning mutagenesis of the β‐sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on β‐sheet formation

B. Matthews, W. Baase, Z. A. Wood, 2004, Protein science : a publication of the Protein Society.

Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme.

B. Matthews, W. Baase, Mohammad S Yousef, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Repacking the Core of T4 lysozyme by automated design.

Stephen L Mayo, Brian W Matthews, S. L. Mayo, 2003, Journal of molecular biology.

Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site.

B. Matthews, W. Baase, X. Zhang, 2000, Protein engineering.

Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme.

I R Vetter, B. Matthews, C. Bustamante, 2000, Proceedings of the National Academy of Sciences of the United States of America.

The introduction of strain and its effects on the structure and stability of T4 lysozyme.

B. Matthews, W. Baase, B W Matthews, 1999, Journal of molecular biology.

Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability.

B. Matthews, W. Baase, L. Weaver, 1999, Journal of molecular biology.

Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site.

B. Matthews, L. Weaver, R. Kuroki, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.

B. Matthews, W. Baase, M. Sagermann, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Converting T4 Phage Lysozyme into a Transglycosidase

B. Matthews, K. Morimoto, RYOTA KUROKI, 1998, Annals of the New York Academy of Sciences.

Generation of ligand binding sites in T4 lysozyme by deficiency-creating substitutions.

B. Matthews, W. Baase, X. Zhang, 1998, Journal of molecular biology.

Isolation and characterization of multiple-methionine mutants of T4 lysozyme with simplified cores

B. Matthews, B. Shoichet, W. Baase, 1997 .

Control of the Catalytic Mechanism of an Enzyme by Amino Acid Substitution

B. Matthews, Keiichi Morimoto, RYOTA KUROKI, 1996, Annals of the New York Academy of Sciences.

The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme.

B. Matthews, W. Baase, E. Baldwin, 1994, Science.

Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability

Philip Pjura, B. Matthews, M. Matsumura, 1993, Protein science : a publication of the Protein Society.

Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme

B. Matthews, H. Nicholson, D. Tronrud, 1992, Biopolymers.

Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.

J A Wozniak, E Söderlind, U. Sauer, 1991, Journal of molecular biology.

Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein.

B. Matthews, M. Matsumura, J. A. Wozniak, 1990, Biochemistry.

A mutant T4 lysozyme (Val 131 → Ala) designed to increase thermostability by the reduction of strain within an α‐helix

B. Matthews, S. Dao-pin, W. Baase, 1990, Proteins.

An oscillation data collection system for high‐resolution protein crystallography

B. Matthews, M. Schmid, D. Ohlendorf, 1981 .

A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme.

B. Matthews, W. Baase, N. Gassner, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Structure of a stabilizing disulfide bridge mutant that closes the active‐site cleft of T4 lysozyme

B. Matthews, M. Matsumura, H. R. Faber, 1992, Protein science : a publication of the Protein Society.

Mutational analysis of protein stability

B. Matthews, 1991 .

Evaluation at atomic resolution of the role of strain in destabilizing the temperature‐sensitive T4 lysozyme mutant Arg 96 → His

B. Matthews, D. Tronrud, B. Mooers, 2009, Protein science : a publication of the Protein Society.

40 – ENGINEERING OF MULTIPLE DISULFIDE BONDS DRAMATICALLY STABILIZES T4 LYSOZYME

B. Matthews, M. Matsumura, G. Signor, 1990 .

Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein.

B. Matthews, D. P. Sun, T. Alber, 1987, Biochemistry.

Selected and Directed Mutants of T4 Phage Lysozyme

B. Matthews, J. A. Wozniak, E. Baker, 1987 .

Amino acid substitutions far from the active site of bacteriophage T4 lysozyme reduce catalytic activity and suggest that the C-terminal lobe of the enzyme participates in substrate binding.

B. Matthews, M. Grütter, 1982, Journal of molecular biology.

Molecular basis of thermostability in the lysozyme from bacteriophage T4

B. Matthews, M. Grütter, MARKUS G. GRÜTTER, 1979, Nature.

Structure of the lysozyme from bacteriophage T4: an electron density map at 2.4 A resolution.

B. Matthews, L. T. Ten Eyck, S. Remington, 1978, Journal of molecular biology.

Long-distance conformational changes in a protein engineered by modulated sequence duplication

B. Matthews, M. Sagermann, L. Gay, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity.

B. Matthews, D. Ohlendorf, D. Tronrud, 1998, Journal of molecular biology.

Structural and genetic analysis of protein folding and stability: Current Opinion in Sturctural Biology 1993, 3:589–593

B. Matthews, 1993 .

Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties

B. Matthews, J. A. Wozniak, L. McIntosh, 1993, Proteins.

Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths

B. Matthews, K. Wilson, J. Bell, 1991, Proteins.

Structural and genetic analysis of electrostatic and other interactions in bacteriophage T4 lysozyme.

J A Wozniak, B. Matthews, H. Nicholson, 1991, Ciba Foundation symposium.

18 – Approaches toward the Design of Proteins of Enhanced Thermostability

B. Matthews, M. Matsumura, H. Nicholson, 1990 .

Crystallographic and Genetic Approaches Toward the Design of Proteins of Enhanced Thermostability

B. Matthews, M. Matsumura, H. Nicholson, 1990 .

Crystallization of mutant lysozymes from bacteriophage T4

B. Matthews, J. A. Wozniak, R. Brennan, 1988 .

Letter: crystallographic data fro lysoxyme from bacteriophage T4.

B. Matthews, F. Dahlquist, A. Maynard, 1973, Journal of molecular biology.

Structural and genetic analysis of the folding and function of T4 lysozyme

B. Matthews, Brian W. Matthews, 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Studies on protein stability with T4 lysozyme.

B. Matthews, B W Matthews, 1995, Advances in protein chemistry.

Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent

B. Matthews, B W Matthews, P Pjura, 1993, Protein science : a publication of the Protein Society.

Crystallography in the Life Sciences

B. Matthews, 1987 .

X-ray Crystallographic Studies of Proteins

B. Matthews, 1976 .

Atomic coordinates for T4 phage lysozyme.

S J Remington, B. Matthews, S. Remington, 1977, Biochemical and biophysical research communications.

A computer controlled film scanner for X-ray crystallography

C. E. Klopfenstein, B. Matthews, P. Colman, 1972 .

Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH.

B. Matthews, R. Brennan, M. M. Dixon, 1991, International journal of biological macromolecules.

Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?

B. Matthews, B W Matthews, M M Dixon, 1989, Biochemistry.

Structure of a mercaptan-thermolysin complex illustrates mode of inhibition of zinc proteases by substrate-analogue mercaptans.

B. Matthews, A. Monzingo, B W Matthews, 1982, Biochemistry.

Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence.

B. Matthews, W. Baase, D. Heinz, 1992, Proceedings of the National Academy of Sciences of the United States of America.

How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme.

B. Matthews, W. Baase, F. Dahlquist, 1993, Nature.

4 – X-Ray Structure of Proteins

B. Matthews, 1977 .

The Conformation of the ε- and γ-Subunits within theEscherichia coli F1 ATPase*

B. Matthews, A. Hausrath, R. Capaldi, 2001, The Journal of Biological Chemistry.

Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography.

B. Matthews, A. Hausrath, G. Grüber, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme.

B. Matthews, W. Baase, X. Zhang, 1991, Biochemistry.

Dissection of protein structure and folding by directed mutagenesis.

U. Sauer, B. Matthews, W. Baase, 1992, Faraday discussions.

Can proteins be turned inside-out?

B. Matthews, 1995, Nature Structural Biology.

Flexible‐geometry conformational energy maps for the amino acid residue preceding a proline

B. Matthews, J. Hurley, David A. Mason, 1992, Biopolymers.

internal sites in T4 lysozyme Structural and thermodynamic analysis of the binding of solvent at

B. Matthews, W. Baase, Michael L. Quillin, 2008 .

Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme

B. Matthews, W. Baase, Michael L. Quillin, 2001, Protein Science.

Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme.

B. Matthews, Michael L. Quillin, W. A. Breyer, 2000, Journal of molecular biology.

Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins.

B. Matthews, T M Gray, B W Matthews, 1984, Journal of molecular biology.

Structure of the nucleocapsid-binding domain from the mumps virus polymerase; an example of protein folding induced by crystallization.

B. Matthews, L. Gay, R. Kingston, 2008, Journal of molecular biology.

Nice guys needn't finish last

B. Matthews, 1997, Nature Structural Biology.

Rare earths as isomorphous calcium replacements for protein crystallography.

B. Matthews, P. Colman, L. Weaver, 1972, Biochemical and biophysical research communications.

A systematic approach to the comparison of protein structures.

S J Remington, B. Matthews, S. Remington, 1980, Journal of molecular biology.

Type II restriction endonucleases: structural, functional and evolutionary relationships.

B. Matthews, R. Kovall, 1999, Current opinion in chemical biology.

Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor

B. Matthews, D. Beckett, L. Weaver, 2001, Protein science : a publication of the Protein Society.

Beta-sheet models for the ordered filamentous structure formed by a peptide that enhances the action of insulin.

B. Matthews, L. Weaver, J. Stagsted, 1996, Journal of structural biology.

The role of calcium ions in the stability and instability of a thermolysin‐like protease

G. Vriend, B. Matthews, V. Eijsink, 2011, Protein science : a publication of the Protein Society.

Crystals of luciferase from Vibrio harveyi. A preliminary characterization.

B. Matthews, L. Weaver, S. Remington, 1985, The Journal of biological chemistry.

A structure for thermolysin.

B. Matthews, K. Titani, P. Colman, 1972, Nature.

Structure of a green bacteriochlorophyll protein

B. Matthews, R. Fenna, 1980 .

Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59.

U. Sauer, B. Matthews, W. Baase, 1992, Biochemistry.

Structural studies of protein-nucleic acid interactions.

B. Matthews, D. Ohlendorf, 1983, Annual review of biophysics and bioengineering.

The structural basis for enhanced stability and reduced DNA binding seen in engineered second-generation Cro monomers and dimers.

B. Matthews, P. Rupert, M. Mossing, 2000, Journal of molecular biology.

Determination of solvent content in cavities in IL-1β using experimentally phased electron density

B. Matthews, P. Wingfield, Michael L. Quillin, 2006, Proceedings of the National Academy of Sciences.

Halogenated benzenes bound within a non-polar cavity in T4 lysozyme provide examples of I...S and I...Se halogen-bonding.

Brian W Matthews, B. Matthews, W. Baase, 2009, Journal of molecular biology.

Atomic CO-ordinates for tosyl-α-chymotrypsin

B. Matthews, D. Blow, J. Birktoft, 1969 .

Kinetic and spectroscopic characterization of the H178A methionyl aminopeptidase from Escherichia coli.

B. Matthews, W. Lowther, A. Copik, 2003, Biochemistry.

Covalent structure of a group-specific protease from rat small intestine. Appendix: crystallographic data for a group specific protease from rat intestine.

B. Matthews, K. Titani, N. Katunuma, 1978, Biochemistry.

Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography.

Gerhard Hummer, Sol M Gruner, Brian W Matthews, 2007, Journal of molecular biology.

Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation.

Gerhard Hummer, Sol M Gruner, Brian W Matthews, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Hydrophobic packing in T4 lysozyme probed by cavity-filling mutants.

B. Matthews, M. Matsumura, W. Baase, 1989, Proceedings of the National Academy of Sciences of the United States of America.

The structure and stability of thermolysin.

B. Matthews, L. T. Ten Eyck, L. Weaver, 1976, Experientia. Supplementum.

Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent.

B. Matthews, W. Baase, M. Blaber, 1995, Journal of molecular biology.

Crystallization of beta-galactosidase does not reduce the range of activity of individual molecules.

Brian W Matthews, B. Matthews, D. Juers, 2003, Biochemistry.

Cryo-cooling in macromolecular crystallography: advantages, disadvantages and optimization

B. Matthews, D. Juers, 2004, Quarterly Reviews of Biophysics.

Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces.

B. Matthews, A. Barkan, Haralambos Hadjivassiliou, 2005, Journal of molecular biology.

Bifunctional abietadiene synthase: mutual structural dependence of the active sites for protonation-initiated and ionization-initiated cyclizations.

B. Matthews, R. Peters, R. Croteau, 2003, Biochemistry.

Reversible lattice repacking illustrates the temperature dependence of macromolecular interactions.

B. Matthews, D. Juers, 2001, Journal of molecular biology.

Structure of a serine protease from rat mast cells determined from twinned crystals by isomorphous and molecular replacement

Brian W. Matthews, L. H. Weaver, S. J. Remington, 1985 .

EDPDB: a multifunctional tool for protein structure analysis

B. Matthews, Xue-jun Zhang, B. W. Matthews, 1995 .

A general method to assess similarity of protein structures, with applications to T4 bacteriophage lysozyme.

S J Remington, B. Matthews, S. Remington, 1978, Proceedings of the National Academy of Sciences of the United States of America.

Refinement of the structure of human basic fibroblast growth factor at 1.6 Å resolution and analysis of presumed heparin binding sites by selenate substitution

B. Matthews, A. Eriksson, L. Cousens, 1993, Protein science : a publication of the Protein Society.

Different interactions used by Cro repressor in specific and nonspecific DNA binding.

B. Matthews, D. Ohlendorf, W. Anderson, 1988, The Journal of biological chemistry.

Crystal structure of an engineered cro monomer bound nonspecifically to DNA: Possible implications for nonspecific binding by the wild‐type protein

B. Matthews, M. Mossing, R. Albright, 1998, Protein science : a publication of the Protein Society.

Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity.

B. Matthews, A. Morton, B W Matthews, 1995, Biochemistry.

Identification of an SH3-binding motif in a new class of methionine aminopeptidases from Mycobacterium tuberculosis suggests a mode of interaction with the ribosome.

Jun O. Liu, B. Matthews, Michael L. Quillin, 2005, Biochemistry.

Structural basis of Prospero-DNA interaction: implications for transcription regulation in developing cells.

B. Matthews, Mohammad S Yousef, 2005, Structure.

Structure and symmetry of oligomeric enzymes.

B. Matthews, S. Bernhard, 1973, Annual review of biophysics and bioengineering.

Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.

B. Matthews, M. He, B W Matthews, 2000, Biochemistry.

THERMODYNAMIC AND STRUCTURAL COMPENSATION IN ""SIZE-SWITCH"" CORE-REPACKING VARIANTS OF T4 LYSOZYME

B. Matthews, E. Baldwin, O. Hajiseyedjavadi, 1996 .

Use of NMR to Detect Water Within Nonpolar Protein Cavities

B. Matthews, A. Gronenborn, G. Clore, 1995, Science.

The structure of a repressor: crystallographic data for the Cro regulatory protein of bacteriophage lambda.

B. Matthews, H. Echols, W. Anderson, 1979, Journal of molecular biology.

Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties

B. Matthews, J. A. Wozniak, L. McIntosh, 1993, Proteins.

Amino acid residues essential for biological activity of a peptide derived from a major histocompatibility complex class I antigen.

B. Matthews, C. Anfinsen, A. Goldstein, 1993, Proceedings of the National Academy of Sciences of the United States of America.

DNA-binding proteins.

B. Matthews, D. Ohlendorf, W. Anderson, 1983, Science.

Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking.

B. Matthews, D. Heinz, B W Matthews, 1994, Protein engineering.

Five retracted structure reports: Inverted or incorrect?

Brian W Matthews, B. Matthews, 2007, Protein science : a publication of the Protein Society.

Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid.

B. Matthews, T M Gray, B W Matthews, 1988, The Journal of biological chemistry.

Racemic crystallography—Easy crystals and easy structures: What's not to like?

B. Matthews, 2009, Protein science : a publication of the Protein Society.

A review about nothing: Are apolar cavities in proteins really empty?

Brian W Matthews, B. Matthews, Lijun Liu, 2009, Protein science : a publication of the Protein Society.

Lessons from the lysozyme of phage T4

B. Matthews, W. Baase, D. Tronrud, 2010, Protein science : a publication of the Protein Society.

Determination of protein molecular weight, hydration, and packing from crystal density.

B. Matthews, 1985, Methods in enzymology.

Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation.

B. Matthews, W. Baase, S. Gruner, 2008, Biochemistry.

Protein Motifs: the Helix‐Turn‐Helix Motif

B. Matthews, 2007 .

Evaluation at atomic resolution of the role of strain in destabilizing the temperature‐sensitive T4 lysozyme mutant Arg 96 → His

B. Matthews, D. Tronrud, B. Mooers, 2009, Protein science : a publication of the Protein Society.

Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.

U. Sauer, B. Matthews, W. Baase, 1991, Journal of molecular biology.

Hydrophobic Interactions in Proteins

Brian W. Matthews, B. Matthews, 2001 .

Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.

B. Matthews, H. Nicholson, W. Becktel, 1988, Nature.

Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.

B. Matthews, Michael L. Quillin, L. Dubois, 2005, Journal of the American Chemical Society.

Selling candles in a post-Edison world: phasing with noble gases bound within engineered sites.

B. Matthews, Michael L. Quillin, 2003, Acta crystallographica. Section D, Biological crystallography.