title: Crystallization and preliminary crystallographic studies of the FAD domain of corn NADH: nitrate reductase.
abstract: Crystals of the flavin domain of corn nitrate reductase expressed in Escherichia coli have been obtained at room temperature, using sodium citrate as precipitant. The crystals diffract to at least 2.5 A resolution at a synchrotron radiation source. Precession photographs show that they belong to the rhombohedral space group R3 with unit cell dimensions a = b = 145.4 A, c = 47.5 A, alpha = beta = 90 degrees and gamma = 120 degrees. There is one subunit per asymmetric unit which gives a packing density of 3.2 A3/Da, indicating a high solvent content in these crystals.
authors.affiliation: Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
authors.forename: G
authors.initials: G
authors.lastname: Lu
authors.forename: W
authors.initials: W
authors.lastname: Campbell
authors.forename: Y
authors.initials: Y
authors.lastname: Lindqvist
authors.forename: G
authors.initials: G
authors.lastname: Schneider
mesh_terms: D003460:Crystallization; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry* / Q000378:metabolism; D050895:Nitrate Reductase (NADH); D009565:Nitrate Reductases / Q000737:chemistry* / Q000378:metabolism; D014961:X-Ray Diffraction; D003313:Zea mays / Q000201:enzymology*
chemical_list: D005182:Flavin-Adenine Dinucleotide; D009565:Nitrate Reductases; D050895:Nitrate Reductase (NADH)