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

Ivo S. Ridder; Henriëtte J. Rozeboom; Jaap Kingma; Dick B. Janssen; Bauke W. Dijkstra

doi:10.1002/pro.5560041220

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

Ivo S. Ridder, Henriëtte J. Rozeboom, Jaap Kingma, Dick B. Janssen, Bauke W. Dijkstra

Research output: Contribution to journal › Article › Academic › peer-review

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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 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%.

Original language	English
Pages (from-to)	2619-2620
Number of pages	2
Journal	Protein Science
Volume	4
Issue number	12
DOIs	https://doi.org/10.1002/pro.5560041220
Publication status	Published - Dec-1995

Keywords

L-2-HALOACID DEHALOGENASE
PROTEIN CRYSTALS
2-CHLOROACETATE DEGRADATION
XANTHOBACTER AUTOTROPHICUS GJ10
X-RAY CRYSTALLOGRAPHY
HALOALKANE DEHALOGENASE

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@article{2e20a07e9e644a8799c0199462270d12,

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

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 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%.",

keywords = "L-2-HALOACID DEHALOGENASE, PROTEIN CRYSTALS, 2-CHLOROACETATE DEGRADATION, XANTHOBACTER AUTOTROPHICUS GJ10, X-RAY CRYSTALLOGRAPHY, HALOALKANE DEHALOGENASE",

author = "Ridder, {Ivo S.} and Rozeboom, {Henri{\"e}tte J.} and Jaap Kingma and Janssen, {Dick B.} and Dijkstra, {Bauke W.}",

note = "Relation: http://www.rug.nl/gbb/ date_submitted:2009 Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute",

year = "1995",

month = dec,

doi = "10.1002/pro.5560041220",

language = "English",

volume = "4",

pages = "2619--2620",

journal = "Protein Science",

issn = "0961-8368",

publisher = "Wiley",

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T1 - Crystallization and preliminary X-ray analysis of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10

AU - Ridder, Ivo S.

AU - Rozeboom, Henriëtte J.

AU - Kingma, Jaap

AU - Janssen, Dick B.

AU - Dijkstra, Bauke W.

N1 - Relation: http://www.rug.nl/gbb/ date_submitted:2009 Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute

PY - 1995/12

Y1 - 1995/12

N2 - 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%.

AB - 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%.

KW - L-2-HALOACID DEHALOGENASE

KW - PROTEIN CRYSTALS

KW - 2-CHLOROACETATE DEGRADATION

KW - XANTHOBACTER AUTOTROPHICUS GJ10

KW - X-RAY CRYSTALLOGRAPHY

KW - HALOALKANE DEHALOGENASE

U2 - 10.1002/pro.5560041220

DO - 10.1002/pro.5560041220

M3 - Article

SN - 0961-8368

VL - 4

SP - 2619

EP - 2620

JO - Protein Science

JF - Protein Science

IS - 12

ER -

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

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