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

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.

SUBMITTER: Gabrielsen M

PROVIDER: S-EPMC2998365 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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

Gabrielsen Mads M Zetterström Caroline E CE Wang Dai D Beckham Katherine S H KS Elofsson Mikael M Isaacs Neil W NW Roe Andrew J AJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20101125 Pt 12

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. ...[more]

PMID: 21139206

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