Crystallization and preliminary X-ray diffraction analysis of a putative carbon-carbon bond hydrolase from Mycobacterium abscessus 103.

Crystallization and preliminary X-ray diffraction analysis of a putative carbon-carbon bond hydrolase from Mycobacterium abscessus 103.
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来自脓肿分枝杆菌 103 的假定碳-碳键水解酶的结晶和初步 X 射线衍射分析。

DOI:
10.1107/s2053230x15001612
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发表时间:
2015-02
期刊:
Acta Crystallogr F Struct Biol Commun
影响因子:
--
通讯作者:
He, Yong-Xing
He, Yong-Xing
中科院分区:
其他
文献类型:
--
作者:
Zhang, Zhang;Jiang, Yong Liang;Wu, Yi;He, Yong-Xing

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来自脓肿分枝杆菌103 (mPhlG)的PhlG蛋白是一种假定的碳-碳键水解酶,其序列与来自分枝真杆菌的根皮素水解酶有30%的同源性,与来自荧光假单胞菌Pf-5的2,4-二乙酰间苯三酚水解酶有38%的同源性。本文报道了mPhlG的表达、纯化和结晶过程。结晶的沉淀剂为100mm柠檬酸pH 5.0, 1.0 M氯化锂,8%(w/v)聚乙二醇6000。晶体衍射分辨率为1.87 Å,属于空间群P21,晶胞参数a = 71.0, b = 63.4, c = 74.7 Å, α = 90.0, β = 103.2, γ = 90.0°。假设不对称单元中存在两个mPhlG分子,VM计算为2.5 Å(3) Da(-1),对应于溶剂含量为50%。
The PhlG protein from Mycobacterium abscessus 103 (mPhlG), which shares 30% sequence identity with phloretin hydrolase from Eubacterium ramulus and 38% sequence identity with 2,4-diacetylphloroglucinol hydrolase from Pseudomonas fluorescens Pf-5, is a putative carbon-carbon bond hydrolase. Here, the expression, purification and crystallization of mPhlG are reported. Crystals were obtained using a precipitant consisting of 100 mM citric acid pH 5.0, 1.0 M lithium chloride, 8%(w/v) polyethylene glycol 6000. The crystals diffracted to 1.87 Å resolution and belonged to space group P21, with unit-cell parameters a = 71.0, b = 63.4, c = 74.7 Å, α = 90.0, β = 103.2, γ = 90.0°. Assuming the presence of two mPhlG molecules in the asymmetric unit, VM was calculated to be 2.5 Å(3) Da(-1), which corresponds to a solvent content of 50%.
DOI: 10.1107/s0907444910045749
发表时间: 2011-04
期刊: Acta crystallographica. Section D, Biological crystallography
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