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

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‐ChiC89–252) 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 P6122 or P6522, with unit‐cell parameters a = b = 100, c = 243 Å. The calculated Matthews coefficient was approximately 3.2, 2.4 or 1.9 Å3 Da−1 assuming the presence of three, four or five Ra‐ChiC89–252 molecules in the asymmetric unit, respectively.