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Expression, purific...
Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosis
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Gabrielsen, Mads (author)
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- Zetterström, Caroline E (author)
- Umeå universitet,Kemiska institutionen
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Wang, Dai (author)
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Beckham, Katherine S H (author)
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- Elofsson, Mikael (author)
- Umeå universitet,Kemiska institutionen
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Isaacs, Neil W (author)
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Roe, Andrew J (author)
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(creator_code:org_t)
- International Union of Crystallography, 2010
- 2010
- English.
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In: Acta Crystallographica. Section F. - : International Union of Crystallography. - 1744-3091 .- 1744-3091. ; 66:Pt 12, s. 1606-1609
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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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
Publication and Content Type
- ref (subject category)
- art (subject category)
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