title: Cloning, purification, crystallization and preliminary X-ray analysis of a chimeric NADPH-cytochrome P450 reductase.
abstract: NADPH-cytochrome P450 reductase (CPR) is the favoured redox partner of microsomal cytochromes P450. This protein is composed of two flavin-containing domains (FMN and FAD) connected by a structured linker. An active CPR chimera consisting of the yeast FMN and human FAD domains has been produced, purified and crystallized. The crystals belonged to the monoclinic space group C2 and contained one molecule per asymmetric unit. Molecular replacement was performed using the published rat and yeast structures as search models. The initial electron-density maps revealed that the chimeric enzyme had crystallized in a conformation that differed from those of previously solved structures.
authors.affiliation: Laboratoire d'Ingénierie des Protéines Membranaires, CNRS, Gif-sur-Yvette, France.
authors.forename: Louise
authors.initials: L
authors.lastname: Aigrain
authors.forename: Denis
authors.initials: D
authors.lastname: Pompon
authors.forename: Gilles
authors.initials: G
authors.lastname: Truan
authors.forename: Solange
authors.initials: S
authors.lastname: Moréra
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry* / Q000302:isolation & purification*; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae
chemical_list: D011993:Recombinant Fusion Proteins; D009251:NADPH-Ferrihemoprotein Reductase