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Purification, crystallization and preliminary X‐ray crystallographic analysis of chitinase from Bacillus cereus NCTU2
Author(s) -
Kuo ChuehYuan,
Wu YueJin,
Hsieh YinCheng,
Guan HongHsiang,
Tsai HueiJu,
Lin YiHung,
Huang YenChieh,
Liu MingYih,
Li YawKuen,
Chen ChunJung
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106031423
Subject(s) - bacillus cereus , chitinase , crystallization , crystallography , x ray , bacillus (shape) , microbiology and biotechnology , materials science , chemistry , biology , enzyme , biochemistry , bacteria , physics , optics , genetics , organic chemistry
Chitinases (EC 3.2.1.14) are found in a broad range of organisms, including bacteria, fungi and higher plants, and play different roles depending on their origin. A chitinase from Bacillus cereus NCTU2 (ChiNCTU2) capable of hydrolyzing chitin as a carbon and nitrogen nutrient has been identified as a member of the family 18 glycoside hydrolases. ChiNCTU2 of molecular weight 36 kDa has been crystallized using the hanging‐drop vapour‐diffusion method. According to the diffraction of chitinase crystals at 1.10 Å resolution, the crystal belongs to space group P 2 1 , with unit‐cell parameters a = 50.79, b = 48.79, c  = 66.87 Å, β = 99.31°. Preliminary analysis indicates there is one chitinase molecule in the asymmetric unit, with a solvent content of 43.4%.

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