title: Crystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogans.
abstract: Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes electron transfer between NADP(H) and ferredoxin. Here, results are reported of the recombinant expression, purification and crystallization of FNR from Leptospira interrogans, a parasitic bacterium of animals and humans. The L. interrogans FNR crystals belong to a primitive monoclinic space group and diffract to 2.4 angstroms resolution at a synchrotron source.
authors.affiliation: Instituto de Física de São Carlos, Universidade de São Paulo, Av. Trabalhador Saocarlense 400, São Carlos, SP, 13560-970, Brazil.
authors.forename: Alessandro S
authors.initials: AS
authors.lastname: Nascimento
authors.forename: Thiago
authors.initials: T
authors.lastname: Ferrarezi
authors.forename: Daniela L
authors.initials: DL
authors.lastname: Catalano-Dupuy
authors.forename: Eduardo A
authors.initials: EA
authors.lastname: Ceccarelli
authors.forename: Igor
authors.initials: I
authors.lastname: Polikarpov
mesh_terms: D003460:Crystallization; D004579:Electron Transport; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry* / Q000302:isolation & purification*; D005288:Ferredoxins / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D007921:Leptospira interrogans / Q000201:enzymology*; D009249:NADP / Q000378:metabolism; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D005288:Ferredoxins; D005182:Flavin-Adenine Dinucleotide; D009249:NADP; D005287:Ferredoxin-NADP Reductase