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Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei
Author(s): Carpena X, Switala J, Loprasert S, Mongkolsuk S, Fita I, Loewen PC
Source: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY    Volume: 58    Pages: 2184-2186    Part: Part 12    Published: DEC 2002  
Times Cited: 11     References: 15     
Abstract: The bifunctional catalase-peroxidase KatG encoded by the katG gene of Burkholderia pseudomallei has a predicted subunit size of 81.6 kDa. It shows high sequence similarity to other catalase- peroxidases of bacterial, archaebacterial and fungal origin, including 64% identity to KatG from Mycobacterium tuberculosis and lesser sequence similarity to members of the plant peroxidase family. Crystals from this protein were grown in 16-20% PEG 4000, 20% 2-methyl-2,4-pentanediol and 0.1 M sodium citrate pH 5.6 by the hanging-drop vapour-diffusion method at 293 K. These crystals diffracted beyond 1.8 Angstrom resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 100.9, b = 115.6, c = 175.2 Angstrom. The data are consistent with either a monomer or a dimer in the crystal asymmetric unit.
Document Type: Article
Language: English
Reprint Address: Loewen, PC (reprint author), Univ Manitoba, Dept Microbiol, Winnipeg, MB R3T 2N2 Canada
Addresses:
1. Univ Manitoba, Dept Microbiol, Winnipeg, MB R3T 2N2 Canada
2. CSIC, Inst Mol Biol, ES-08034 Barcelona, Spain
3. Chulabhorn Res Inst, Biotechnol Lab, Bangkok 10210, Thailand
Publisher: BLACKWELL MUNKSGAARD, 35 NORRE SOGADE, PO BOX 2148, DK-1016 COPENHAGEN, DENMARK
Subject Category: Biochemical Research Methods; Biochemistry & Molecular Biology; Biophysics; Crystallography
IDS Number: 619GV
ISSN: 0907-4449
DOI: 10.1107/S0907444902017869
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