Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus.
Flavodoxins are small electron-transfer proteins that contain one molecule of noncovalently bound flavin mononucleotide (FMN). The flavodoxin NifF from the photosynthetic bacterium Rhodobacter capsulatus is reduced by one electron from ferredoxin/flavodoxin:NADP(H) reductase and was postulated to be an electron donor to nitrogenase in vivo. NifF was cloned and overexpressed in Escherichia coli, purified and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of PEG 3350 and PEG 400 at pH 5.5 and belong to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 66.49, c = 121.32 A. X-ray data sets have been collected to 2.17 A resolution.
Pérez-Dorado
Inmaculada
I
Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto de Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
Bortolotti
Ana
A
Cortez
Néstor
N
Hermoso
Juan A
JA
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005287:Ferredoxin-NADP Reductase / Q000378:metabolism; D005418:Flavodoxin / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D009586:Nitrogen Fixation; D016354:Rhodobacter capsulatus / Q000201:enzymology*
D005418:Flavodoxin; D005287:Ferredoxin-NADP Reductase