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The structure of an orthorhombic crystal form of a 'forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag.

Acta crystallographica. Section F, Structural biology and crystallization communications - 1 May 2012

Beckham Katherine S H, Byron Olwyn, Roe Andrew J, Gabrielsen Mads

Abstract excerpt

Thiol peroxidase (Tpx) is an atypical 2-Cys peroxiredoxin, which has been suggested to be important for cell survival and virulence in Gram-negative pathogens. The structure of a catalytically inactive version of this protein in an orthorhombic crystal form has been determined by molecular replacement. Structural alignments revealed that Tpx is conserved. Analysis of the crystal packing shows that the linker...

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Identifiers

PMID: 22691780
DOI: 10.1107/S1744309112011487
PMCID: PMC3374505

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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