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

Gabrielsen, Mads (author)
Zetterström, Caroline E (author)
Umeå universitet,Kemiska institutionen
Wang, Dai (author)
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Beckham, Katherine S H (author)
Elofsson, Mikael (author)
Umeå universitet,Kemiska institutionen
Isaacs, Neil W (author)
Roe, Andrew J (author)
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 (creator_code:org_t)
International Union of Crystallography, 2010
2010
English.
In: Acta Crystallographica. Section F. - : International Union of Crystallography. - 1744-3091 .- 1744-3091. ; 66:Pt 12, s. 1606-1609
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Keyword

Yersinia pseudotuberculosis
thiol peroxidases
Tpx
peroxiredoxins

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art (subject category)

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