2FX3

Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set

Summary for 2FX3

Entry DOI	10.2210/pdb2fx3/pdb
Descriptor	Elongation factor Tu, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywords	ef-tu, merohedral twinning, translation
Biological source	Escherichia coli
Cellular location	Cytoplasm: Q83JC4
Total number of polymer chains	1
Total formula weight	43676.78
Authors	Heffron, S.E.,Moeller, R.,Jurnak, F. (deposition date: 2006-02-03, release date: 2006-03-28, Last modification date: 2023-08-30)
Primary citation	Heffron, S.E.,Moeller, R.,Jurnak, F. Solving the structure of Escherichia coli elongation factor Tu using a twinned data set. Acta Crystallogr.,Sect.D, 62:433-438, 2006 Cited by PubMed 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. PubMed: 16552145 DOI: 10.1107/S0907444906004021 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.4 Å)

Structure validation