The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
- 1 September 1993
- journal article
- research article
- Published by Elsevier BV in Structure
- Vol. 1 (1), 35-50
- https://doi.org/10.1016/0969-2126(93)90007-4
Abstract
No abstract availableThis publication has 53 references indexed in Scilit:
- The GTPase superfamily: conserved structure and molecular mechanismNature, 1991
- Induced-fit movements in adenylate kinasesJournal of Molecular Biology, 1990
- How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?Journal of Molecular Biology, 1990
- Between objectivity and subjectivityNature, 1990
- A mutation that prevents GTP-dependent activation of the α chain of GsNature, 1988
- Relation between structure and function of α/β–protejnsQuarterly Reviews of Biophysics, 1980
- Stereochemical course of thiophosphoryl group transfer catalyzed by adenylate kinaseJournal of the American Chemical Society, 1978
- Polymorphism in crystalline elongation factor Tu · GDP from Escherichia coliJournal of Molecular Biology, 1976
- Crystals of partially trypsin-digested elongation factor TuJournal of Molecular Biology, 1976
- Allosteric proteins and cellular control systemsJournal of Molecular Biology, 1963