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Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosis
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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2010 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. 66, no Pt 12, 1606-1609 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
International Union of Crystallography , 2010. Vol. 66, no Pt 12, 1606-1609 p.
Keyword [en]
Yersinia pseudotuberculosis, thiol peroxidases, Tpx, peroxiredoxins
Identifiers
URN: urn:nbn:se:umu:diva-38733DOI: 10.1107/S1744309110039679ISI: 000285064800014PubMedID: 21139206OAI: oai:DiVA.org:umu-38733DiVA: diva2:381290
Available from: 2010-12-27 Created: 2010-12-27 Last updated: 2017-12-11Bibliographically approved

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