2fx3
From Proteopedia
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| , resolution 3.400Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set
Overview
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.
About this Structure
2FX3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solving the structure of Escherichia coli elongation factor Tu using a twinned data set., Heffron SE, Moeller R, Jurnak F, Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):433-8. Epub 2006, Mar 18. PMID:16552145
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