Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/75783
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dc.contributor.authorPang, X.-
dc.contributor.authorXu, F.-
dc.contributor.authorBell, S.-
dc.contributor.authorGuo, D.-
dc.contributor.authorWong, L.-
dc.contributor.authorRao, Z.-
dc.date.issued2007-
dc.identifier.citationActa Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2007; 63(4):342-345-
dc.identifier.issn1744-3091-
dc.identifier.issn1744-3091-
dc.identifier.urihttp://hdl.handle.net/2440/75783-
dc.description.abstractCytochrome 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.-
dc.description.statementofresponsibilityXiaoyun Pang, Feng Xu, Stephen G. Bell, Delin Guo, Luet-Lok Wong and Zihe Rao-
dc.language.isoen-
dc.publisherBlackwell Munksgaard-
dc.rights© International Union of Crystallography 2007-
dc.subjectcytochrome P450 203A1-
dc.subjectRhodopseudomonas palustris-
dc.titlePurification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris-
dc.typeJournal article-
dc.identifier.doi10.1107/S1744309107012705-
pubs.publication-statusPublished-
dc.identifier.orcidBell, S. [0000-0002-7457-9727]-
Appears in Collections:Aurora harvest
Chemistry and Physics publications

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