Crystal structure at 1.2Aresolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase
- 1 August 1997
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 16 (15) , 4760-4769
- https://doi.org/10.1093/emboj/16.15.4760
Abstract
EMBO Press is an editorially independent publishing platform for the development of EMBO scientific publications.Keywords
This publication has 32 references indexed in Scilit:
- Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 Å resolutionJournal of Molecular Biology, 1997
- Solution Structure of the Anticodon-binding Domain of Escherichia coli Lysyl-tRNA Synthetase and Studies of its Interaction with tRNALysJournal of Molecular Biology, 1995
- MC-Fit: Using Monte-Carlo methods to get accurate confidence limits on enzyme parametersBioinformatics, 1994
- Mapping of the Zinc Binding Domain of Escherichia coli Methionyl-tRNA SynthetaseJournal of Molecular Biology, 1993
- Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNAfMet formyltransferaseJournal of Molecular Biology, 1992
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Fast and sensitive multiple sequence alignments on a microcomputerBioinformatics, 1989
- Genetic engineering of methionyl-tRNA synthetase: in vitro regeneration of an active synthetase by proteolytic cleavage of a methionyl-tRNA synthetase-β-galactosidase chimeric proteinBiochimie, 1988
- Binding of zinc to Escherichia coli phenylalanyl-tRNA synthetase. Comparison with other aminoacyl-tRNA synthetasesBiochemistry, 1981
- Peptidyl-transfer RNA hydrolase prevents inhibition of protein synthesis initiationNature, 1978