自养黄色杆菌GJ10来源的L-2-卤代酸脱卤酶的结晶及初步X射线分析
Crystallization and preliminary X-ray analysis of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10.
作者信息
Ridder I S, Rozeboom H J, Kingma J, Janssen D B, Dijkstra B W
机构信息
Laboratory of Biophysical Chemistry, University of Groningen, The Netherlands.
出版信息
Protein Sci. 1995 Dec;4(12):2619-20. doi: 10.1002/pro.5560041220.
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%.
卤代酸脱卤酶是一类能裂解2-卤代链烷酸中碳-氯或碳-溴键的酶。利用宏观接种技术，已在室温下从20%聚乙二醇8000、200 mM甲酸钠（pH 6.8 - 7.0）中培养出了来自自养黄色杆菌GJ10（能降解1,2-二氯乙烷）的L-2-卤代酸脱卤酶的X射线级晶体。这些晶体在X射线束中能衍射至2.0 Å分辨率，属于空间群C2221。晶胞参数为a = 58.8 Å，b = 93.1 Å，c = 84.2 Å。已收集到分辨率为2.3 Å的天然数据集，完整性为97%，Rsym为6.0%。
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