Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosis

Gabrielsen, M. , Zetterström, C.E., Wang, D., Beckham, K.S.H., Elofsson, M., Isaacs, N.W. and Roe, A. (2010) Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosis. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 66(12), pp. 1606-1609. (doi: 10.1107/S1744309110039679) (PMID:21139206) (PMCID:PMC2998365)

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Abstract

Thiol peroxidase is an atypical 2-Cys peroxiredoxin that reduces alkyl hydroperoxides. Wild-type and C61S mutant protein have been recombinantly expressed in Escherichia coli and purified using nickel-affinity chromatography. Initial crystallization trials yielded three crystal forms in three different space groups (P2(1), P6(4) and P2(1)2(1)2(1)) both in the presence and the absence of DTT.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Wang, Mr Dai and Gabrielsen, Dr Mads and Roe, Professor Andrew and Isaacs, Professor Neil
Authors: Gabrielsen, M., Zetterström, C.E., Wang, D., Beckham, K.S.H., Elofsson, M., Isaacs, N.W., and Roe, A.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
College of Science and Engineering > School of Chemistry
Journal Name:Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
Publisher:Wiley-Blackwell Publishing, Inc.
ISSN:1744-3091
ISSN (Online):1744-3091

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
491441A biochemical and molecular analysis of the YhaO membrane protein in Escherichia coli O157:H7Andrew RoeBiotechnology and Biological Sciences Research Council (BBSRC)BB/G011389/1Infection Immunity and Inflammation Life Sciences