Overproduction, purification, crystallization and preliminary X-ray analysis of the peroxiredoxin domain of a larger natural hybrid protein from Thermotoga maritima

Journal Article · Tue Jan 01 00:00:00 EST 2008 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309107064391· OSTI ID:22360471

Barbey, Carole ^[1]; Rouhier, Nicolas ^[2]; Haouz, Ahmed ^[3]; Navaza, Alda ^[1]; Jacquot, Jean-Pierre ^[2]

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1. Laboratoire de Biophysique Moléculaire, Cellulaire et Tissulaire, UMR 7033, Université Paris 13, UFR SMBH, 74 Rue Marcel Cachin, 93017 Bobigny CEDEX (France)
2. Unité Mixte de Recherches 1136 INRA UHP (Interaction Arbres Microorganismes), IFR 110, Nancy Université BP 239, 54506 Vandoeuvre-lès-Nancy CEDEX (France)
3. Plate-forme de Cristallogenèse et Diffraction des Rayons X, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris (France)

Crystals of the peroxiredoxin domain of a larger natural hybrid protein from T. maritima were obtained which diffracted to 2.9 Å resolution on a synchrotron source. Thermotoga maritima contains a natural hybrid protein constituted of two moieties: a peroxiredoxin domain at the N-terminus and a nitroreductase domain at the C-terminus. The peroxiredoxin (Prx) domain has been overproduced and purified from Escherichia coli cells. The recombinant Prx domain, which is homologous to bacterial Prx BCP and plant Prx Q, folds properly into a stable protein that possesses biological activity. The recombinant protein was crystallized and synchrotron data were collected to 2.9 Å resolution. The crystals belonged to the tetragonal space group I422, with unit-cell parameters a = b = 176.67, c = 141.20 Å.

• OSTI ID: 22360471
• Journal Information: Acta Crystallographica. Section F, Vol. 64, Issue Pt 1; Other Information: PMCID: PMC2374002; PMID: 18097097; PUBLISHER-ID: rp5010; OAI: oai:pubmedcentral.nih.gov:2374002; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
ESCHERICHIA COLI
HYBRIDIZATION
PROTEINS
RESOLUTION
SPACE GROUPS
SYNCHROTRONS