Open AccessCrystallization and preliminary X‐ray diffraction studies of the catalytic domain of a novel chitinase, a member of GH family 23, from the moderately thermophilic bacterium Ralstonia sp. A‐471
Author(s) -
Okazaki Nobuo,
Arimori Takao,
Nakazawa Masami,
Miyatake Kazutaka,
Ueda Mitsuhiro,
Tamada Taro
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111004751
Subject(s) - thermophile , chitinase , crystallization , crystallography , bacteria , domain (mathematical analysis) , catalysis , diffraction , x ray crystallography , materials science , chemistry , microbiology and biotechnology , biochemistry , biology , enzyme , organic chemistry , physics , genetics , optics , mathematical analysis , mathematics
Chitinase from the moderately thermophilic bacterium Ralstonia sp. A‐471 (Ra‐ChiC) is divided into two domains: a chitin‐binding domain (residues 36–80) and a catalytic domain (residues 103–252). Although the catalytic domain of Ra‐ChiC has homology to goose‐type lysozyme, Ra‐ChiC does not show lysozyme activity but does show chitinase activity. The catalytic domain with part of an interdomain loop (Ra‐ChiC 89–252 ) was crystallized under several different conditions using polyethylene glycol as a precipitant. The crystals diffracted to 1.85 Å resolution and belonged to space group P 6 1 22 or P 6 5 22, with unit‐cell parameters a = b = 100, c = 243 Å. The calculated Matthews coefficient was approximately 3.2, 2.4 or 1.9 Å 3 Da −1 assuming the presence of three, four or five Ra‐ChiC 89–252 molecules in the asymmetric unit, respectively.