title: Crystallization and preliminary X-ray studies of an electron-transfer complex of ferredoxin and ferredoxin-dependent glutamate synthase from the cyanobacterium Leptolyngbya boryana.
abstract: Ferredoxin (Fd) dependent glutamate synthase (Fd-GOGAT) is a key enzyme involved in nitrogen assimilation that catalyzes the two-electron reductive conversion of Gln and 2-oxoglutarate to two molecules of Glu. Fd serves as an electron donor for Fd-GOGAT and the two proteins form a transient electron-transfer complex. In this study, these two proteins were cocrystallized using the hanging-drop vapour-diffusion method. Diffraction data were collected and processed at 2.65 Å resolution. The crystals belonged to space group P4(3), with unit-cell parameters a = b = 84.95, c = 476.31 Å.
authors.affiliation: Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
authors.forename: Kanako
authors.initials: K
authors.lastname: Shinmura
authors.forename: Norifumi
authors.initials: N
authors.lastname: Muraki
authors.forename: Ayako
authors.initials: A
authors.lastname: Yoshida
authors.forename: Toshiharu
authors.initials: T
authors.lastname: Hase
authors.forename: Genji
authors.initials: G
authors.lastname: Kurisu
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000201:enzymology*; D005288:Ferredoxins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding
chemical_list: D005288:Ferredoxins; D000594:Amino Acid Oxidoreductases; C042233:glutamate synthase (ferredoxin)