Crystallization and preliminary crystallographic analysis of poly-gamma-glutamate hydrolase from bacteriophage PhiNIT1

噬菌体 PhiNIT1 的多聚γ-谷氨酸水解酶的结晶及初步晶体学分析

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Abstract

Particular Bacillus subtilis strains produce a capsular polypeptide poly-gamma-glutamate (gamma-PGA) that functions as a physical barrier against bacteriophage infection. Bacteriophage PhiNIT1 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 A using a synchrotron X-ray source and were found to belong to space group P3(1)21 or P3(2)21.

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