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Crystallization and preliminary structure analysis of CobE, an essential protein of cobalamin (vitamin B12) biosynthesis. | LitMetric

Crystallization and preliminary structure analysis of CobE, an essential protein of cobalamin (vitamin B12) biosynthesis.

Acta Crystallogr Sect F Struct Biol Cryst Commun

Department of Chemistry, University of York, Heslington, York YO10 5YW, England.

Published: April 2005

AI Article Synopsis

Article Abstract

CobE, a protein implicated in vitamin B12 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(1)2(1)2(1), with unit-cell parameters a = 31.86, b = 41.07, c = 87.41 A. The diffraction extends to a resolution of 1.9 A. 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 A. The anomalous measurements will be used for phasing.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952438PMC
http://dx.doi.org/10.1107/S1744309105006731DOI Listing

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