J. Kraut

J. Kraut, S. Oatley, J. E. Villafranca, 1986, Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences.

Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide.

J. Kraut, Jimin Wang, M. Miller, 1993, Biochemistry.

The molecular weight of a-chymotrypsinogen

R. D. Wade, J. Kraut, H. Neurath, 1957 .

CHYMOTRYPSINOGEN: A THREE-DIMENSIONAL FOURIER SYNTHESIS AT 5 å RESOLUTION

J. Kraut, S. Freer, L. Sieker, 1962 .

Crystal structure of a subtilisin BPN' complex with N-benzoyl-L-arginine.

J. Kraut, C. Wright, R. A. Alden, 1972, Journal of molecular biology.

Synthesis of Caged NAD(P)+ Coenzymes: Photorelease of NADP+

J. Kraut, D. Magde, C. P. Salerno, 1997 .

Dihydrofolate reductase: x-ray structure of the binary complex with methotrexate.

N. Xuong, J. Bolin, D. Matthews, 1977, Science.

Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I.

J. Kraut, M. Miller, Mark A Miller, 1994, Biochemistry.

X-ray crystallographic study of boronic acid adducts with subtilisin BPN' (Novo). A model for the catalytic transition state.

D. Matthews, J. Kraut, S. Freer, 1975, The Journal of biological chemistry.

Structure of the iron-sulfur cluster in the Chromatius iron protein at 2.25 Angstrom resolution.

N. Xuong, J. Kraut, C. Carter, 1972, Cold Spring Harbor symposia on quantitative biology.

On the identity of subtilisins BPN' and Novo.

J. Kraut, J. Robertus, R. A. Alden, 1971, Biochemical and biophysical research communications.

Identification of the most rapidly iodinating tyrosine in subtilisin BPN.

J. Kraut, B. Weber, 1968, Biochemical and biophysical research communications.

Reaction of horse cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I.

J. Kraut, M. Miller, Mark A Miller, 1994, Biochemistry.

Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome c.

J. Kraut, G. Tollin, M. Miller, 1988, Biochemistry.

Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy.

J. Kraut, A. English, T. Spiro, 1988, Biochemistry.

Reaction of ferrous cytochrome c peroxidase with dioxygen: site-directed mutagenesis provides evidence for rapid reduction of dioxygen by intramolecular electron transfer from the compound I radical site.

J. Kraut, M. Miller, T. Traylor, 1992, Biochemistry.

Comparison of oxidation-reduction site geometries in oxidized and reduced Chromatium high potential iron protein and oxidized Peptococcus aerogenes ferredoxin.

J. Kraut, C. Carter, S. Freer, 1974, The Journal of biological chemistry.

Crystallization and purification of the enzyme anthranilate phosphoribosyl transferase.

N. Xuong, J. Kraut, V. Ashford, 1988, Journal of molecular biology.

Crystal Structure of Adenosine-5′-phosphate

J. Kraut, L. H. Jensen, 1960, Nature.

Long-range structural effects in a second-site revertant of a mutant dihydrofolate reductase.

J. Kraut, K. Brown, E. Howell, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Pi-, delta-, and gamma-chymotrypsin: three-dimensional electron-density and difference maps at 5 A resolution, and comparison with chymotrypsinogen.

J. Kraut, S. Freer, H. Wright, 1967, Proceedings of the National Academy of Sciences of the United States of America.

Role of aspartate 27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPH.

J. Kraut, Raymond L. Blakley, E. Howell, 1990, The Journal of biological chemistry.

CO dissociation in cytochrome c peroxidase: site-directed mutagenesis shows that distal Arg 48 influences CO dissociation rates.

J. Kraut, M. Miller, M. Coletta, 1990, Biochemistry.

CO recombination in cytochrome c peroxidase: effect of the local heme environment on CO binding explored through site-directed mutagenesis.

J. Kraut, M. Miller, M. Coletta, 1990, Biochemistry.

Comparison of the -, - and -chymotrypsin family with -chymotrypsin.

J. Kraut, H. Wright, P. E. Wilcox, 1968, Journal of molecular biology.

CHYMOTRYPSINOGEN: INCREASED RESOLUTION AND ABSOLUTE CONFIGURATION.

J. Kraut, L. Sieker, D. F. High, 1964, Proceedings of the National Academy of Sciences of the United States of America.

The crystal structure of myo-inositol

J. Kraut, I. Rabinovich, 1964 .

Isolation and partial characterization of iodinated chymotrypsinogens.

J. Kraut, B. Weber, 1968, Biochemical and biophysical research communications.

Effect of Asp-235-->Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase.

J. Kraut, M. Miller, J. Erman, 1992, Biochemistry.

Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding.

Christopher Bystroff, J. Kraut, C. Bystroff, 1994, Biochemistry.

Role of aspartate 27 in the binding of methotrexate to dihydrofolate reductase from Escherichia coli.

J. Kraut, Raymond L. Blakley, E. Howell, 1988, The Journal of biological chemistry.

Polypeptide halomethyl ketones bind to serine proteases as analogs of the tetrahedral intermediate. X-ray crystallographic comparison of lysine- and phenylalanine-polypeptide chloromethyl ketone-inhibited subtilisin.

J. Kraut, T. Poulos, S. Freer, 1976, The Journal of biological chemistry.

The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.

B C Finzel, J. Kraut, T. Poulos, 1985, The Journal of biological chemistry.

Dihydrofolate reductase. The stereochemistry of inhibitor selectivity.

J M Burridge, J. Bolin, D. Filman, 1985, The Journal of biological chemistry.

Crystal structure of nitric oxide inhibited cytochrome c peroxidase.

J. Kraut, T. Poulos, S. Edwards, 1988, Biochemistry.

The crystal structure of thiamine hydrochloride (vitamin B)

J. Kraut, H. Reed, 1962 .

The stereochemistry of peroxidase catalysis.

J. Kraut, T. Poulos, 1980, The Journal of biological chemistry.

Crystal structures of chicken liver dihydrofolate reductase: binary thioNADP+ and ternary thioNADP+.biopterin complexes.

J. Kraut, M. McTigue, B. Kaufman, 1993, Biochemistry.

Exploring the molecular mechanism of dihydrofolate reductase.

J. Kraut, K. Brown, 1992, Faraday discussions.

Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state.

S J Oatley, J. Kraut, C. Bystroff, 1990, Biochemistry.

X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis.

N. Xuong, J. Kraut, S. Oatley, 1991, Biochemistry.

Crystal structure of cytochrome c peroxidase compound I.

R. Hamlin, J. Kraut, S. Edwards, 1987, Biochemistry.

Structural bases for function in cytochromes c. An interpretation of comparative x-ray and biochemical data.

J. Kraut, F. Salemme, M. Kamen, 1973, The Journal of biological chemistry.

Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c.

J. Kraut, H. Pelletier, J Kraut, 1993, Science.

How do enzymes work?

J. Kraut, J Kraut, Joseph Kraut, 1988, Science.

7 Chymotrypsin-Chemical Properties and Catalysis

J. Kraut, 1971 .

Refinement of the crystal structure of adenosine‐5'‐phosphate

J. Kraut, L. H. Jensen, 1963 .

Construction of an altered proton donation mechanism in Escherichia coli dihydrofolate reductase.

J. Kraut, J. E. Villafranca, E. Howell, 1987, Biochemistry.

Recent ENDOR and Pulsed Electron Paramagnetic Resonance Studies of Cytochrome c Peroxidase ‐ Compound I and Its Site‐Directed Mutants

J. Kraut, C. Scholes, M. Farnum, 1989 .

Harunganin: A Crystallographic Determination of an Unknown Structure

J. Kraut, R. A. Alden, G. Stout, 1962 .

Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim.

J M Burridge, C. Beddell, J. Champness, 1985, The Journal of biological chemistry.

Dihydrofolate reductase from Lactobacillus casei. Stereochemistry of NADPH binding.

N. Xuong, D. Matthews, J. Kraut, 1979, The Journal of biological chemistry.

Dihydrofolate reductase from Lactobacillus casei. X-ray structure of the enzyme methotrexate.NADPH complex.

N. Xuong, J. Bolin, D. Filman, 1978, Journal of Biological Chemistry.

Re-examination of the charge relay system in subtilisin comparison with other serine proteases.

D. Matthews, J. Kraut, J. Birktoft, 1977, The Journal of biological chemistry.

The structure of oxidized cytochrome c 2 of Rhodospirillum rubrum.

N. Xuong, J. Kraut, S. Freer, 1976, The Journal of biological chemistry.

The crystal structure of androsterone.

J. Kraut, D. F. High, 1966, Acta crystallographica.

Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate.

J. Kraut, V. Ashford, J. Davies, 1990, Biochemistry.

Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I.

J. Kraut, K. Brown, M. Miller, 1993, Biochemistry.

Investigation of the functional role of tryptophan-22 in Escherichia coli dihydrofolate reductase by site-directed mutagenesis.

J. Kraut, K. Brown, E. Howell, 1994, Biochemistry.

A hypothetical model of the cytochrome c peroxidase . cytochrome c electron transfer complex.

J. Kraut, T. Poulos, J Kraut, 1980, The Journal of biological chemistry.

The crystal structure of cytochrome c peroxidase.

N. Xuong, J. Kraut, T. Poulos, 1980, The Journal of biological chemistry.

Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications.

J. Kraut, R. Callender, Raymond L. Blakley, 1994, Biochemistry.

Hybridization, conjugation, and bond lengths. An experimental test

J. Kraut, R. A. Alden, T. Traylor, 1967 .

Atomic coordinates for subtilisin BPN' (or Novo).

J. Kraut, J. Birktoft, J. Robertus, 1971, Biochemical and biophysical research communications.

Subtilisin BPN': Tertiary Structure and Inhibitor Binding

J. Kraut, C. Wright, R. A. Alden, 1970 .

Subtilisin; a stereochemical mechanism involving transition-state stabilization.

J. Kraut, J. Birktoft, J. Robertus, 1972, Biochemistry.

Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution.

B C Finzel, J. Kraut, T. Poulos, 1984, The Journal of biological chemistry.

STRUCTURAL STUDIES WITH X-RAYS.

J. Kraut, 1965, Annual review of biochemistry.

Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism.

Samuel H. Wilson, J. Kraut, M. Sawaya, 1994, Science.

A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase beta.

J. Kraut, M. Sawaya, S. H. Wilson, 1996, Biochemistry.

Directed mutagenesis of dihydrofolate reductase.

J. Kraut, R. Ogden, J. E. Villafranca, 1983, Science.

Enzyme-DNA Interactions Required for Efficient Nucleotide Incorporation and Discrimination in Human DNA Polymerase β(*)

Samuel H. Wilson, T. Kunkel, J. Kraut, 1996, The Journal of Biological Chemistry.

5 Chymotrypsinogen: X-Ray Structure

J. Kraut, 1971 .

Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts.

J. Kraut, A. English, T. Spiro, 1988, Biochemistry.

Single-crystal resonance Raman spectroscopy of site-directed mutants of cytochrome c peroxidase.

J. Kraut, T. Spiro, G. Smulevich, 1990, Biochemistry.

Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation.

J. Kraut, G. Tollin, T. Meyer, 1988, Biochemistry.

Yeast cytochrome c peroxidase: mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I.

J. Kraut, J. E. Villafranca, L. Fishel, 1987, Biochemistry.

Detection of an oxyferryl porphyrin pi-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound I.

J. Kraut, J. Erman, L. Vitello, 1989, Biochemistry.

An engineered disulfide bond in dihydrofolate reductase.

N. Xuong, J. Kraut, S. Oatley, 1987, Biochemistry.

Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin.

J. Kraut, M. McTigue, B. Kaufman, 1992, Biochemistry.

Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase.

J. Kraut, M. Miller, T. Spiro, 1991, Biochemistry.

A cation binding motif stabilizes the compound I radical of cytochrome c peroxidase.

J. Kraut, G. Han, M. Miller, 1994, Proceedings of the National Academy of Sciences of the United States of America.

2.2 Å structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex

J. Kraut, A. Shaw, Mark A Miller, 1994, Nature Structural Biology.

Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.

J. Kraut, J. Satterlee, J. Erman, 1990, Biochemistry.

Chymotrypsinogen: 2,5-Å crystal structure, comparison with α-chymotrypsin, and implications for zymogen activation

N. Xuong, J. Kraut, S. Freer, 1970 .

An x-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPN'.

J. Kraut, J. Birktoft, J. Robertus, 1972, Biochemistry.

Dihydrofolate Reductase (DHFR)

J. Kraut, M. Sawaya, 2002 .

Structure and function of alternative proton-relay mutants of dihydrofolate reductase.

J. Kraut, S. Oatley, J. E. Villafranca, 1992, Biochemistry.

Crystal structure of a novel trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67.

D. Baccanari, D. Matthews, J. Kraut, 1986, Biochemistry.

Crystal structure of avian dihydrofolate reductase containing phenyltriazine and NADPH.

C. Hansch, D. Matthews, J. Kraut, 1982, The Journal of biological chemistry.

Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding.

J. Kraut, C. Bystroff, J Kraut, 1994, Biochemistry.

Nuclear magnetic resonance study of the state of protonation of inhibitors bound to mutant dihydrofolate reductase lacking the active-site carboxyl.

J. Kraut, R. London, Raymond L. Blakley, 1986, Biochemistry.

The electrostatic potential of Escherichia coli dihydrofolate reductase

J. Kraut, A. Hagler, David H. Kitson, 1991, Proteins.

Electron redistribution on binding of a substrate to an enzyme: Folate and dihydrofolate reductase

Jürgen Bajorath, Jan Andzelm, George Fitzgerald, 1991, Proteins.

A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27----serine Escherichia coli dihydrofolate reductase.

J. Kraut, E. Howell, M. S. Warren, 1990, Biochemistry.

Analysis of hydride transfer and cofactor fluorescence decay in mutants of dihydrofolate reductase: possible evidence for participation of enzyme molecular motions in catalysis.

J. Kraut, J. Grimsley, D. Magde, 1991, Biochemistry.

Changes in the electron density of the cofactor NADPH on binding to E. coli dihydrofolate reductase

J. Kraut, A. Hagler, J. Bajorath, 1991, Proteins.

The aromatic substrate binding site in subtilisin BPN' and its resemblance to chymotrypsin.

J. Kraut, J. Birktoft, J. Robertus, 1972, Cold Spring Harbor symposia on quantitative biology.

HUMAN DNA POLYMERASE BETA COMPLEXED WITH NICKED DNA

J. Kraut, M. Sawaya, S. H. Wilson, 1997 .

Structure of subtilisin BPN' at 2.5 angström resolution.

J. Kraut, C. Wright, R. A. Alden, 1969, Nature.

Molecular geometry of cytochrome c and its peroxidase: a model for biological electron transfer.

J. Kraut, 1981, Biochemical Society transactions.

The crystal structure of fluoride-inhibited cytochrome c peroxidase.

J. Kraut, T. Poulos, S. Edwards, 1984, The Journal of biological chemistry.

Mechanism of single-bond shortening. Evidence from the crystal structures of 1-biapocamphane, 1-binorbornane, and 1-biadamantane

J. Kraut, R. A. Alden, T. Traylor, 1968 .

Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II.

J. Kraut, G. Han, M. Miller, 1994, Biochemistry.

15 Subtilisin: X-Ray Structure

J. Kraut, J. Kraut, 1971 .

Crystallographic structure refinement of Chromatium high potential iron protein at two Angstroms resolution.

J. Kraut, C. Carter, S. Freer, 1975, The Journal of biological chemistry.

A hydrogen-bond network at the active site of subtilisin BPN'.

J. Kraut, C. Wright, R. A. Alden, 1970, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Active-site mutations in cytochrome c peroxidase : a critical role for histidine-52 in the rate of formation of compound I

J. Kraut, Mark A Miller, J. Erman, 1992 .

The density of gold-silver-copper alloys and its calculation from the chemical composition

W. B. Stern, J. Kraut, 2000 .

Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase.

N. Xuong, R. Hamlin, J. Kraut, 1978, The Journal of biological chemistry.

Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications.

J. Kraut, M. Sawaya, K. Brown, 1995, Biochemistry.

Crystal structures of D,L-homocysteine thiolactone hydrochloride: two polymorphic forms and a hybrid.

J. Kraut, S. Freer, 1965, Acta crystallographica.

Compound I radical in site-directed mutants of cytochrome c peroxidase as probed by electron paramagnetic resonance and electron-nuclear double resonance.

J. Kraut, C. Scholes, X. Tan, 1991, Biochemistry.

Characterization of the hydrogen peroxide-enzyme reaction for two cytochrome c peroxidase mutants.

J. Kraut, J. Erman, L. Vitello, 1990, Biochimica et biophysica acta.

Crystal structures of Escherichia coli dihydrofolate reductase complexed with 5-formyltetrahydrofolate (folinic acid) in two space groups: evidence for enolization of pteridine O4.

J. Kraut, V. M. Reyes, J Kraut, 1996, Biochemistry.

A proposed model for interaction of polypeptides with RNA.

J. Kraut, C. Carter, 1974, Proceedings of the National Academy of Sciences of the United States of America.

The shape of the chymotrypsinogen molecule from x-ray diffraction.

J. Kraut, J KRAUT, 1958, Biochimica et biophysica acta.

The Crystal Structure of Cytochrome c Peroxidase at 2.5 Å Resolution

N. Xuong, J. Kraut, T. Poulos, 1982 .

Atomic coordinates for ferricytochrome c2 of Rhodospirillum rubrum.

J. Kraut, S. Freer, F. Salemme, 1973, Biochemical and biophysical research communications.

Rapid measurement of large numbers of reflection intensities for proteins

J. Kraut, S. Freer, C. Wright, 1968 .

The molecular and crystal structure of the plant pigment harunganin

J. Kraut, R. A. Alden, G. Stout, 1964 .