2fx3

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|PDB= 2fx3 |SIZE=350|CAPTION= <scene name='initialview01'>2fx3</scene>, resolution 3.400&Aring;
|PDB= 2fx3 |SIZE=350|CAPTION= <scene name='initialview01'>2fx3</scene>, resolution 3.400&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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[[Category: merohedral twinning]]
[[Category: merohedral twinning]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:57:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:07:53 2008''

Revision as of 13:07, 23 March 2008


PDB ID 2fx3

Drag the structure with the mouse to rotate
, resolution 3.400Å
Ligands: and
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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