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 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.
University of California, Irvine, USA.
Susan E
SE
Heffron
Rhonda
R
Moeller
Frances
F
Jurnak
D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000737:chemistry*; D006153:Guanosine Diphosphate / Q000737:chemistry; D008274:Magnesium / Q000737:chemistry; D008958:Models, Molecular; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D000900:Anti-Bacterial Agents; D006153:Guanosine Diphosphate; D010444:Peptide Elongation Factor Tu; D008274:Magnesium