CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER-AUTOTROPHICUS GJ10

Citation
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
Citations number
14
Categorie Soggetti
Biology
Journal title
ISSN journal
09618368
Volume
4
Issue
12
Year of publication
1995
Pages
2619 - 2620
Database
ISI
SICI code
0961-8368(1995)4:12<2619:CAPAOL>2.0.ZU;2-N
Abstract
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%.