Crystallization 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.

ABSTRACT: 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 P6(1)22 or P6(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.

SUBMITTER: Okazaki N 

PROVIDER: S-EPMC3080159 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature