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Crystallization and preliminary structure analysis of CobE, an essential protein of cobalamin (vitamin B{sub 12}) biosynthesis

Journal Article · · Acta Crystallographica. Section F
 [1]; ; ;  [2]
  1. Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW (United Kingdom)
  2. School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS (United Kingdom)
P. aeruginosa CobE, a protein implicated in vitamin B{sub 12} biosynthesis, has been crystallized and data on the native and SeMet forms recorded to resolutions of 1.9 and 1.7 Å, respectively. The anomalous measurements will be used for phasing. CobE, a protein implicated in vitamin B{sub 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 P2{sub 1}2{sub 1}2{sub 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.
OSTI ID:
22356126
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 4 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English

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