Open AccessCrystallization and preliminary X‐ray analysis of the catalase–peroxidase KatG from Burkholderia pseudomallei
Author(s) -
Carpena Xavier,
Switala Jack,
Loprasert Suvit,
Mongkolsuk Skorn,
Fita Ignacio,
Loewen Peter C.
Publication year - 2002
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444902017869
Subject(s) - peroxidase , dimer , catalase , chemistry , crystallization , crystallography , protein subunit , microbiology and biotechnology , biology , enzyme , biochemistry , gene , organic chemistry
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 Å resolution and belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 100.9, b = 115.6, c = 175.2 Å. The data are consistent with either a monomer or a dimer in the crystal asymmetric unit.