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

Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):433-8. doi: 10.1107/S0907444906004021. Epub 2006 Mar 18.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • 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


  • Anti-Bacterial Agents
  • Guanosine Diphosphate
  • Peptide Elongation Factor Tu
  • Magnesium