title: 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.
authors.affiliation: Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084, People's Republic of China.
authors.forename: Ying
authors.initials: Y
authors.lastname: Peng
authors.forename: Feng
authors.initials: F
authors.lastname: Xu
authors.forename: Stephen G
authors.initials: SG
authors.lastname: Bell
authors.forename: Luet-Lok
authors.initials: LL
authors.lastname: Wong
authors.forename: Zihe
authors.initials: Z
authors.lastname: Rao
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D010088:Oxidoreductases / Q000737:chemistry*; D011487:Protein Conformation; D012241:Rhodopseudomonas / Q000201:enzymology*
chemical_list: D010088:Oxidoreductases; C028878:ferredoxin-NAD+ reductase