Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/75783
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Type: Journal article
Title: Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris
Author: Pang, X.
Xu, F.
Bell, S.
Guo, D.
Wong, L.
Rao, Z.
Citation: Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2007; 63(4):342-345
Publisher: Blackwell Munksgaard
Issue Date: 2007
ISSN: 1744-3091
1744-3091
Statement of
Responsibility: 
Xiaoyun Pang, Feng Xu, Stephen G. Bell, Delin Guo, Luet-Lok Wong and Zihe Rao
Abstract: Cytochrome P450 enzymes constitute a large family of haemoproteins that catalyze the monooxygenation of a great variety of endogenous and exogenous organic compounds. Cytochrome P450 203A1 (CYP203A1, RPA1009) from the metabolically versatile organism Rhodopseudomonas palustris binds a broad range of substrates, in particular substituted aromatic compounds. Crystals of CYP203A1 suitable for X-ray crystallography have been obtained and diffraction data were collected in-house to 2.0 Å resolution from a single crystal. The crystals belong to space group P222, with unit-cell parameters a = 40.1, b = 95.1, c = 99.0 Å, [alpha] = [beta] = [gamma] = 90°. There is one protein molecule per asymmetric unit.
Keywords: cytochrome P450 203A1
Rhodopseudomonas palustris
Rights: © International Union of Crystallography 2007
DOI: 10.1107/S1744309107012705
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Chemistry and Physics publications

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