Beckham, K. S.H., Byron, O. , Roe, A. J. and Gabrielsen, M. (2012) 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, 68(5), pp. 522-526. (doi: 10.1107/S1744309112011487) (PMID:22691780) (PMCID:PMC3374505)
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Abstract
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 region of the affinity tag is important for formation of the crystal lattice.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Gabrielsen, Dr Mads and Roe, Professor Andrew and Byron, Professor Olwyn |
| Authors: | Beckham, K. S.H., Byron, O., Roe, A. J., and Gabrielsen, M. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Infection & Immunity |
| Journal Name: | Acta Crystallographica. Section F: Structural Biology and Crystallization Communications |
| Publisher: | International Union of Crystallography |
| ISSN: | 1744-3091 |
| Copyright Holders: | Copyright © 2012 International Union of Crystallography |
| First Published: | First published in Acta Crystallographica. Section F: Structural Biology and Crystallization Communications 68(5):522-526 |
| Publisher Policy: | Reproduced in accordance with the copyright policy of the publisher |
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