title: Crystallization and preliminary X-ray analysis of geraniol dehydrogenase from Backhousia citriodora (lemon myrtle).
abstract: A recombinant form of geraniol dehydrogenase (EC 1.1.1.183) from Backhousia citriodora was overexpressed in Escherichia coli and purified and crystallized by the sitting-drop method using polyethylene glycol 3350 as a precipitant. A data set to 2.3 Å resolution was collected from a monocrystal at 98 K using synchrotron radiation on beamline NE3A of the Photon Factory. The crystals belonged to the orthorhombic group P2(1)2(1)2, with unit-cell parameters a = 125.00, b = 151.01, c = 51.18 Å. The asymmetric unit is expected to contain two BcGEDH molecules, with a corresponding crystal volume per protein weight of 3.1 Å(3) Da(-1) and a solvent content of 60.6%.
authors.affiliation: Department of Food and Nutritional Sciences, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka, Yada 52-1, Suruga-ku, Shizuoka, Japan.
authors.forename: Yosuke
authors.initials: Y
authors.lastname: Saito
authors.forename: Sohei
authors.initials: S
authors.lastname: Ito
authors.forename: Anna M
authors.initials: AM
authors.lastname: Koltunow
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Sakai
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D027822:Myrtaceae / Q000201:enzymology*; D010088:Oxidoreductases / Q000737:chemistry*
chemical_list: D010088:Oxidoreductases