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Crystallization and preliminary X‐ray analysis of L‐2‐haloacid dehalogenase from xanthobacter autotrophicus GJ10
Author(s) -
Ridder Ivo S.,
Rozeboom Henriëtte J.,
Dijkstra Bauke W.,
Kingma Jaap,
Janssen Dick B.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560041220
Subject(s) - chemistry , crystallization , crystallography , organic chemistry
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 Å resolution, belong to the spacegroup C222 1 . Cell parameters are a = 58.8 Å, b = 93.1 Å, c = 84.2 Å. A native data set to 2.3 Å has been collected, with a completeness of 97% and an R sym of 6.0%.