Crystallization and preliminary crystallographic analysis of poly-γ-glutamate hydrolase from bacteriophage ΦNIT1

Particular Bacillus subtilis strains produce a capsular polypeptide poly-γ-glutamate (γ-PGA) that functions as a physical barrier against bacteriophage infection. Bacteriophage ΦNIT1 can infect B. subtilis and produces a novel γ-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 Å using a synchrotron X-ray source and were found to belong to space group P3₁21 or P3₂21.