Solving the structure of Escherichia coli elongation factor Tu using a twinned data set

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 Å in space group P3121, with unit‐cell parameters a...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2006-04, Vol.62 (4), p.433-438
Hauptverfasser:	Heffron, Susan E., Moeller, Rhonda, Jurnak, Frances
Format:	Artikel
Sprache:	eng
Schlagworte:	Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - metabolism Binding Sites crystal mosaicity Crystallization Crystallography, X-Ray Dimerization elongation factor Tu epitaxial twinning Escherichia coli Escherichia coli - chemistry Guanosine Diphosphate - chemistry Magnesium - chemistry merohedral twinning Models, Molecular Peptide Elongation Factor Tu - chemistry Peptide Elongation Factor Tu - metabolism Protein Binding Protein Structure, Tertiary
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