Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

[1]  Michael G. Rossmann,et al.  Chemical and biological evolution of a nucleotide-binding protein , 1974, Nature.

[2]  A. J. Furth,et al.  Studies on the subunit structure and amino acid sequence of trisoe phosphate isomerase from chicken breast muscle. , 1974, The Biochemical journal.

[3]  J. Harris,et al.  Triose phosphate isomerase from the coelacanth. An approach to the rapid determination of an amino acid sequence with small amounts of material. , 1974, The Biochemical journal.

[4]  P. Y. Chou,et al.  Prediction of protein conformation. , 1974, Biochemistry.

[5]  M G Rossmann,et al.  Comparison of super-secondary structures in proteins. , 1973, Journal of molecular biology.

[6]  Cyrus Chothia,et al.  Conformation of twisted β-pleated sheets in proteins , 1973 .

[7]  G. Petsko,et al.  A low‐temperature device for protein crystallography , 1973 .

[8]  P. Corran,et al.  The amino acid sequence of rabbit muscle triose phosphate isomerase , 1973, FEBS letters.

[9]  R. Offord,et al.  Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine. , 1972, The Biochemical journal.

[10]  R. Offord.  The possible use of cyanogen bromide fragments in the semisynthesis of proteins and polypeptides. , 1972, The Biochemical journal.

[11]  J. W. Campbell,et al.  X-ray diffraction studies on enzymes in the glycolytic pathway. , 1972, Cold Spring Harbor symposia on quantitative biology.

[12]  G. Petsko,et al.  Crystallographic studies of chicken triose phosphate isomerase. , 1972, Cold Spring Harbor symposia on quantitative biology.

[13]  M. Vijayan,et al.  The determination and refinement of heavy‐atom parameters in protein heavy‐atom derivatives. Some model calculations using acentric reflexions , 1971 .

[14]  S. G. Waley,et al.  The active centre of rabbit muscle triose phosphate isomerase. The site that is labelled by glycidol phosphate. , 1971, The Biochemical journal.

[15]  F. C. Hartman.  Haloacetol phosphates. Characterization of the active site of rabbit muscle triose phosphate isomerase. , 1971, Biochemistry.

[16]  R. Wolfenden,et al.  Changes in absorption spectrum and crystal structure of triose phosphate isomerase brought about by 2-phosphoglycollate, a potential transition state analogue. , 1970, Journal of molecular biology.

[17]  D. Trentham,et al.  A new class of chromophoric organomercurials and their reactions with D-glyceraldehyde 3-phosphate dehydrogenase. , 1969, The Biochemical journal.

[18]  Portland Press Ltd.  IUPAC-IUB Commission on Biochemical Nomenclature. A one-letter notation for amino acid sequences. Tentative rules. , 1969, The Journal of biological chemistry.

[19]  F M Richards,et al.  The matching of physical models to three-dimensional electron-density maps: a simple optical device. , 1968, Journal of molecular biology.

[20]  R. Scopes.  Methods for starch-gel electrophoresis of sarcoplasmic proteins. An investigation of the relative mobilities of the glycolytic enzymes from the muscles of a variety of species. , 1968, The Biochemical journal.

[21]  L. Johnson,et al.  Preliminary crystallographic data for triose phosphate isomerase , 1967 .

[22]  G Kartha,et al.  Combination of multiple isomorphous replacement and anomalous dispersion data for protein structure determination. 3. Refinement of heavy atom positions by the least-squares method. , 1965, Acta crystallographica.

[23]  D. Blow,et al.  A means of promoting heavy-atom binding in protein crystals. , 1965, Journal of molecular biology.

[24]  A. North,et al.  The combination of isomorphous replacement and anomalous scattering data in phase determination of non-centrosymmetric reflexions , 1965 .

[25]  A. North,et al.  Adaptation of a linear diffractometer to measure three X-ray reflections quasi-simultaneously , 1964 .

[26]  M. Perutz,et al.  The structure of haemoglobin VIII. A three-dimensional Fourier synthesis at 5.5 Å resolution: determination of the phase angles , 1961, Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences.

[27]  F. Crick,et al.  The treatment of errors in the isomorphous replacement method , 1959 .

[28]  S. Waley,et al.  The action of trypsin on polylysine. , 1953, The Biochemical journal.