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Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide.

Authors
Type
Published Article
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
1744-3091
Publisher
International Union of Crystallography
Publication Date
Volume
63
Issue
Pt 7
Pages
571–575
Identifiers
PMID: 17620713
Source
Medline
License
Unknown

Abstract

The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity. Crystals of WrbA holoprotein in complex with the oxidized flavin cofactor (FMN) were obtained using standard vapour-diffusion techniques. Deep yellow tetragonal crystals obtained from differing crystallization conditions display different space groups and unit-cell parameters. X-ray crystal structures of the WrbA holoprotein have been determined to resolutions of 2.0 and 2.6 A.

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