PMID:16552145

Citation	Heffron, SE, Moeller, R and Jurnak, F (2006) Solving the structure of Escherichia coli elongation factor Tu using a twinned data set. Acta Crystallogr. D Biol. Crystallogr. 62:433-8
Abstract	Escherichia coli elongation factor Tu-GDP (EF-Tu-GDP) was crystallized in the presence of novel inhibitors. The only crystals which could be grown were epitaxially as well as merohedrally twinned, highly mosaic and diffracted to a resolution of 3.4 A in space group P3(1)21, with unit-cell parameters a = b = 69.55, c = 169.44 A, alpha = beta = 90, gamma = 120 degrees . To determine whether an inhibitor was present in the crystal, a poor-quality X-ray diffraction data set had to be processed. The three-dimensional structure was ultimately solved and the original question answered. The results also reveal a new type of dimer packing for EF-Tu-GDP.
Links	PubMed Online version:10.1107/S0907444906004021
Keywords	Anti-Bacterial Agents/chemistry; Anti-Bacterial Agents/metabolism; Binding Sites; Crystallization; Crystallography, X-Ray; Dimerization; Escherichia coli/chemistry; Guanosine Diphosphate/chemistry; Magnesium/chemistry; Models, Molecular; Peptide Elongation Factor Tu/chemistry; Peptide Elongation Factor Tu/metabolism; Protein Binding; Protein Structure, Tertiary
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