Preparation, crystallization and preliminary X-ray analysis of XC2382, an ApaG protein of unknown structure from Xanthomonas campestris
Preparation, crystallization and preliminary X-ray analysis of XC2382, an ApaG protein of unknown structure from Xanthomonas campestris
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DOI：
10.1107/s1744309105018956
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发表时间：
2005-07-01
影响因子：
0.9
通讯作者：
Chou, SH
中科院分区：
文献类型：
--
作者：
Chin, KH;Chou, CC;Chou, SH
野油菜黄单胞菌 pv. Campestris 是黑腐病的病原体，黑腐病是世界范围内十字花科作物的主要病害之一。它的基因组编码大约 4500 种蛋白质，其中大约三分之一的功能未知。 XC2382 就是这样一种蛋白质，分子量为 14.2 kDa。根据生物信息学研究，它被注释为具有多种功能的ApaG基因产物。 ApaG 蛋白已在大肠杆菌中过表达，并使用悬滴蒸气扩散法进行纯化和结晶。晶体衍射分辨率至少为 2.30 埃。它们是四方晶系，属于空间群 P4(1/3)，晶胞参数 a = b = 57.6，c = 122.9 埃。不对称单元中有两个、三个或四个分子。
Xanthomonas campestris pv. campestris is the causative agent of black rot, one of the major worldwide diseases of cruciferous crops. Its genome encodes approximately 4500 proteins, roughly one third of which have unknown function. XC2382 is one such protein, with a MW of 14.2 kDa. Based on a bioinformatics study, it was annotated as an ApaG gene product that serves multiple functions. The ApaG protein has been overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to a resolution of at least 2.30 angstrom. They are tetragonal and belong to space group P4(1/3), with unit-cell parameters a = b = 57.6, c = 122.9 angstrom. There are two, three or four molecules in the asymmetric unit.