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Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/75515
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dc.contributor.authorPeng, Y.-
dc.contributor.authorXu, F.-
dc.contributor.authorBell, S.-
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(5):422-425-
dc.identifier.issn1744-3091-
dc.identifier.issn1744-3091-
dc.identifier.urihttp://hdl.handle.net/2440/75515-
dc.description.abstractPalustrisredoxin reductase from Rhodopseudomonas palustris CGA009, a member of the oxygenase-coupled NADH-dependent ferredoxin reductase (ONFR) family, catalyzes electron transfer from NADH to ferredoxins. It is an essential component of the cytochrome P450 systems in R. palustris CGA009, a model organism with diverse metabolic pathways. Here, the crystallization of palustrisredoxin reductase is reported. The crystals belong to the trigonal space group P3₂21, with unit-cell parameters a = 107.5, b = 107.5, c = 69.9 Å, and diffract to 2.2 Å resolution on a synchrotron source.-
dc.description.statementofresponsibilityYing Peng, Feng Xu, Stephen G. Bell, Luet-Lok Wong and Zihe Rao-
dc.language.isoen-
dc.publisherBlackwell Munksgaard-
dc.rights© International Union of Crystallography 2007-
dc.source.urihttp://dx.doi.org/10.1107/s1744309107017411-
dc.subjectpalustrisredoxin reductase-
dc.subjectferredoxin reductases-
dc.titleCrystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009-
dc.typeJournal article-
dc.identifier.doi10.1107/S1744309107017411-
pubs.publication-statusPublished-
dc.identifier.orcidBell, S. [0000-0002-7457-9727]-
Appears in Collections:Aurora harvest
Chemistry and Physics publications

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