A low-resolution model of crystalline methionyl-transfer RNA synthetase from Escherichia coli
- 1 March 1976
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 102 (1), 93-101
- https://doi.org/10.1016/0022-2836(76)90075-9
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenaseJournal of Molecular Biology, 1974
- Repeated sequences in methionyl‐tRNA synthetase from E. coliFEBS Letters, 1974
- The structure of horse liver alcohol dehydrogenaseFEBS Letters, 1974
- The Mechanism of Action of Methionyl-tRNA Synthetase from Escherichia coli. Mechanism of the Amino-Acid Activation Reaction Catalyzed by the Native and the Trypsin-Modified EnzymesEuropean Journal of Biochemistry, 1974
- Structure of horse muscle phosphoglycerate kinase: Some results on the chain conformation, substrate binding and evolution of the molecule from a 3 Å Fourier mapJournal of Molecular Biology, 1974
- Polypeptide conformation of cytoplasmic malate dehydrogenase from an electron density map at 3.0 Å resolutionJournal of Molecular Biology, 1972
- Modification of Methionyl‐tRNA Synthetase by Proteolytic Cleavage and Properties of the Trypsin‐Modified EnzymeEuropean Journal of Biochemistry, 1971
- On the relative scaling of X-ray photographsActa Crystallographica, 1965
- The crystal structure of myoglobin: Phase determination to a resolution of 2 Å by the method of isomorphous replacementActa Crystallographica, 1961
- The treatment of errors in the isomorphous replacement methodActa Crystallographica, 1959