Crystallization and preliminary X-ray analysis of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10

Haloacid dehalogenases are enzymes that cleave carbon-chlorine or carbon-bromine bonds of 2-haloalkanoates. X-ray-quality crystals of L-2-haloacid dehalogenase from the 1,2-dichloroethane-degrading bacterium Xanthobacter autotrophicus GJ10 have been grown at room temperature from 20% PEG 8000, 200 mM sodium formate at pH 6.8-7.0, using macroseeding techniques. The crystals, which diffract in the X-ray beam up to 2.0 Angstrom resolution, belong to the spacegroup C222(1). Cell parameters are a = 58.8 Angstrom, b = 93.1 Angstrom, c = 84.2 Angstrom. A native data set to 2.3 Angstrom has been collected, with a completeness of 97% and an R(sym) of 6.0%