Open AccessCrystallization and preliminary X‐ray analysis of geraniol dehydrogenase from Backhousia citriodora (lemon myrtle)
Author(s) -
Saito Yosuke,
Ito Sohei,
Koltunow Anna M.,
Sakai Hiroshi
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111006920
Subject(s) - orthorhombic crystal system , polyethylene glycol , crystallization , crystallography , synchrotron radiation , chemistry , escherichia coli , nuclear chemistry , solvent , materials science , crystal structure , organic chemistry , biochemistry , optics , physics , gene
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 P 2 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%.