Structural features of the GDP binding site of elongation factor Tu fromEscherichia colias determined by X-ray diffraction
Open Access
- 29 June 1981
- journal article
- Published by Wiley in FEBS Letters
- Vol. 129 (1) , 177-179
- https://doi.org/10.1016/0014-5793(81)80784-3
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- X‐ray determination of the GDP‐binding site of Escherichia coli elongation factor Tu by substitution with ppGppFEBS Letters, 1981
- Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolutionJournal of Molecular Biology, 1981
- Relation between structure and function of α/β–protejnsQuarterly Reviews of Biophysics, 1980
- The Complete Amino-Acid Sequence of Elongation Factor Tu from Escherichia coliEuropean Journal of Biochemistry, 1980
- High resolution X-ray crystallographic analysis of a modified form of the elongation factor Tu:Guanosine diphosphate complexJournal of Molecular Biology, 1978
- Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-Tu, from Escherichia coliJournal of Molecular Biology, 1977
- On the relative scaling of X-ray photographsActa Crystallographica, 1965