Is. Ridder et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER-AUTOTROPHICUS GJ10, Protein science, 4(12), 1995, pp. 2619-2620
Haloacid dehalogenases are enzymes that cleave carbon-chlorine or carb
on-bromine bonds of 2-haloalkanoates. X-ray-quality crystals of L-2-ha
loacid dehalogenase from the 1,2-dichloroethane-degrading bacterium Xa
nthobacter 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 9
7% and an R(sym) of 6.0%.