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Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009.

ABSTRACT: Palustrisredoxin 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 P3(2)21, with unit-cell parameters a = 107.5, b = 107.5, c = 69.9 A, and diffract to 2.2 A resolution on a synchrotron source.

SUBMITTER: Peng Y

PROVIDER: S-EPMC2335014 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009.

Peng Ying Y Xu Feng F Bell Stephen G SG Wong Luet-Lok LL Rao Zihe Z

Acta crystallographica. Section F, Structural biology and crystallization communications 20070420 Pt 5

Palustrisredoxin 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 P3(2)21, with unit-cell parameters a = 107. ...[more]

PMID: 17565187

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