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%.