Crystallization and preliminary crystallographic analysis of poly-γ-glutamate hydrolase from bacteriophage ΦNIT1
Crystallization and preliminary crystallographic analysis of poly-γ-glutamate hydrolase from bacteriophage ΦNIT1
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DOI：
10.1107/s1744309109029881
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发表时间：
2009-09-01
影响因子：
0.9
通讯作者：
Kimura, Keitarou
中科院分区：
文献类型：
--
作者：
Fujimoto, Zui;Shiga, Isao;Kimura, Keitarou
特定的枯草芽孢杆菌菌株产生荚膜多肽聚-γ-谷氨酸（γ-PGA），其作为抵抗噬菌体感染的物理屏障。噬菌体 Phi NIT1 可以感染枯草芽孢杆菌并产生新型 γ-PGA 水解酶 PghP。通过坐滴蒸气扩散法过表达、纯化和结晶PghP。使用同步加速器X射线源将晶体衍射至分辨率为2.4埃，发现晶体属于空间群P3(1)21或P3(2)21。
Particular Bacillus subtilis strains produce a capsular polypeptide poly-gamma-glutamate (gamma-PGA) that functions as a physical barrier against bacteriophage infection. Bacteriophage Phi NIT1 can infect B. subtilis and produces a novel gamma-PGA hydrolase PghP. PghP was overexpressed, purified and crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.4 angstrom using a synchrotron X-ray source and were found to belong to space group P3(1)21 or P3(2)21.