Crystallization and preliminary structure analysis of CobE, an essential protein of cobalamin (vitamin B{sub 12}) biosynthesis
- Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW (United Kingdom)
- 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, Vol. 61, Issue Pt 4; Other Information: PMCID: PMC1952438; PMID: 16511064; PUBLISHER-ID: za5094; OAI: oai:pubmedcentral.nih.gov:1952438; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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