title: Crystallization and preliminary X-ray diffraction studies of a NADH oxidase from Thermus thermophilus HB8.
abstract: The thermophile NADH oxidase from Thermus thermophilus, cloned and expressed in Escherichia coli, has been purified to homogeneity and crystallized. Three different crystal forms were found to be suitable for X-ray diffraction analysis. Crystals of the tetragonal form, grown in the presence of 25% polyethylene glycol 4000 and 0.25 M-NaCl at pH 6.6, were chosen for further analysis. These crystals belong to the space group P4(1)(3)2(1)2 with refined lattice constants of a = 94.8 A and c = 49.0 A, indicating a cell content of one monomer per asymmetric unit of the crystal. The crystals diffract to a resolution of 2.2 A.
authors: GBF, Gesellschaft für Biotechnologische Forschung mbH, Braunschweig, Germany.
authors: H
authors: H
authors: Erdmann
authors: H J
authors: HJ
authors: Hecht
authors: H J
authors: HJ
authors: Park
authors: M
authors: M
authors: Sprinzl
authors: D
authors: D
authors: Schomburg
authors: R D
authors: RD
authors: Schmid
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli; D009097:Multienzyme Complexes / Q000737:chemistry*; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D016963:Thermus thermophilus / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D009097:Multienzyme Complexes; D011994:Recombinant Proteins; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases