Open AccessCrystallization and preliminary crystallographic analysis of poly‐γ‐glutamate hydrolase from bacteriophage ΦNIT1
Author(s) -
Fujimoto Zui,
Shiga Isao,
Itoh Yoshifumi,
Kimura Keitarou
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109029881
Subject(s) - bacteriophage , crystallization , bacillus subtilis , resolution (logic) , biology , crystallography , diffusion , materials science , biophysics , chemistry , escherichia coli , biochemistry , bacteria , physics , genetics , organic chemistry , artificial intelligence , computer science , gene , thermodynamics
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 P 3 1 21 or P 3 2 21.