title: Crystallization and preliminary crystallographic analysis of poly-gamma-glutamate hydrolase from bacteriophage PhiNIT1.
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.
authors.affiliation: National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, Japan.
authors.forename: Zui
authors.initials: Z
authors.lastname: Fujimoto
authors.forename: Isao
authors.initials: I
authors.lastname: Shiga
authors.forename: Yoshifumi
authors.initials: Y
authors.lastname: Itoh
authors.forename: Keitarou
authors.initials: K
authors.lastname: Kimura
mesh_terms: D017103:Bacillus Phages / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006867:Hydrolases / Q000737:chemistry*; D011099:Polyglutamic Acid / Q000031:analogs & derivatives* / Q000378:metabolism
chemical_list: C511775:poly(gamma-glutamic acid); D011099:Polyglutamic Acid; D006867:Hydrolases