title: Crystallization and preliminary X-ray diffraction studies on a soluble Escherichia coli quinone oxidoreductase.
abstract: Single crystals suitable for X-ray diffraction studies have been obtained from a soluble Escherichia coli NAD(P)H-dependent quinone oxidoreductase (QOR) of molecular mass 35 kDa. Crystals were grown by the vapour diffusion method in the presence of NADPH and diffract strongly to beyond 2.0 A. The space group was determined to be P2(1)2(1)2(1) with unit cell dimensions of a = 107.44 A, b = 104.06 A, c = 77.45 A. There is one dimer in the asymmetric unit.
authors.affiliation: Centre for Molecular Structure and Function, Research School of Chemistry, Australian National University, Canberra.
authors.forename: K J
authors.initials: KJ
authors.lastname: Edwards
authors.forename: J M
authors.initials: JM
authors.lastname: Thorn
authors.forename: J A
authors.initials: JA
authors.lastname: Daniher
authors.forename: N E
authors.initials: NE
authors.lastname: Dixon
authors.forename: D L
authors.initials: DL
authors.lastname: Ollis
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D011808:Quinone Reductases / Q000737:chemistry*
chemical_list: D011808:Quinone Reductases