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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 |
Published version: | http://dx.doi.org/10.1107/s1744309107012705 |
Appears in Collections: | Aurora harvest Chemistry and Physics publications |
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