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 Å resolution and belong to space group P212121, 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.
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CITATION STYLE
Carpena, X., Switala, J., Loprasert, S., Mongkolsuk, S., Fita, I., & Loewen, P. C. (2002). Crystallization and preliminary X-ray analysis of the catalase-peroxidase KatG from Burkholderia pseudomallei. Acta Crystallographica Section D: Biological Crystallography, 58(12), 2184–2186. https://doi.org/10.1107/S0907444902017869
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