Open AccessCrystallization and preliminary structure analysis of CobE, an essential protein of cobalamin (vitamin B 12 ) biosynthesis
Author(s) -
Graham Ross M.,
Raux Evelyne,
Warren Martin J.,
Vévodová Jitka,
Wilson Keith S.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105006731
Subject(s) - cobalamin , crystallization , biosynthesis , chemistry , vitamin b , biochemistry , crystallography , vitamin , vitamin b12 , organic chemistry , enzyme
CobE, a protein implicated in vitamin B 12 biosynthesis, from Pseudomonas aeruginosa has been overexpressed in Escherichia coli , purified and crystallized using hanging‐drop vapour diffusion. The crystals belong to the primitive orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 31.86, b = 41.07, c = 87.41 Å. The diffraction extends to a resolution of 1.9 Å. There is one molecule per asymmetric unit and the estimated solvent content is 35%. SeMet‐labelled CobE has been prepared and crystallizes under the same conditions as the native protein with diffraction to 1.7 Å. The anomalous measurements will be used for phasing.