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Report No.

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 ${it Ralstonia}$ sp. A-471

Okazaki, Nobuo; Arimori, Takao; Nakazawa, Masami*; Miyatake, Kazutaka*; Ueda, Mitsuhiro*; Tamada, Taro

Chitinase from the moderately thermophilic bacterium ${it Ralstonia}$ 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 ${AA}$ resolution and belonged to space group ${it P}$6$$_{1}$$22 or ${it P}$6$$_{5}$$22, with unit-cell parameters ${it a}$ = ${it b}$ = 100, ${it c}$ = 243 ${AA}$. The calculated Matthews coefficient was approximately 3.2, 2.4 or 1.9 ${AA}$ $$^{3}$$ Da$$^{-1}$$ assuming the presence of three, four or five Ra-ChiC$$_{89-252}$$ molecules in the asymmetric unit, respectively.



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Category:Biochemical Research Methods



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