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

I S Ridder; H J Rozeboom; J Kingma; D B Janssen; B W Dijkstra

doi:10.1002/pro.5560041220

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

Protein Sci. 1995 Dec;4(12):2619-20. doi: 10.1002/pro.5560041220.

Authors

I S Ridder¹, H J Rozeboom, J Kingma, D B Janssen, B W Dijkstra

Affiliation

¹ Laboratory of Biophysical Chemistry, University of Groningen, The Netherlands.

Abstract

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 A resolution, belong to the spacegroup C2221. Cell parameters are a = 58.8 A, b = 93.1 A, c = 84.2 A. A native data set to 2.3 A has been collected, with a completeness of 97% and an Rsym of 6.0%.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Crystallography, X-Ray*
Gram-Negative Aerobic Bacteria / enzymology*
Hydrogen-Ion Concentration
Hydrolases / chemistry*

Substances

Hydrolases
2-haloacid dehalogenase