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蜡样芽孢杆菌NCTU2几丁质酶的纯化、结晶及初步X射线晶体学分析

Purification, crystallization and preliminary X-ray crystallographic analysis of chitinase from Bacillus cereus NCTU2.

作者信息

Kuo Chueh-Yuan, Wu Yue-Jin, Hsieh Yin-Cheng, Guan Hong-Hsiang, Tsai Huei-Ju, Lin Yi-Hung, Huang Yen-Chieh, Liu Ming-Yih, Li Yaw-Kuen, Chen Chun-Jung

机构信息

Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt 9):916-9. doi: 10.1107/S1744309106031423. Epub 2006 Aug 26.

Abstract

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 A resolution, the crystal belongs to space group P2(1), with unit-cell parameters a = 50.79, b = 48.79, c = 66.87 A, beta = 99.31 degrees . Preliminary analysis indicates there is one chitinase molecule in the asymmetric unit, with a solvent content of 43.4%.

摘要

几丁质酶(EC 3.2.1.14)存在于广泛的生物体中,包括细菌、真菌和高等植物,并且根据其来源发挥不同的作用。已鉴定出蜡样芽孢杆菌NCTU2(ChiNCTU2)的一种几丁质酶能够将几丁质水解为碳源和氮源营养物质,它是18家族糖苷水解酶的一员。分子量为36 kDa的ChiNCTU2已通过悬滴气相扩散法结晶。根据几丁质酶晶体在1.10 Å分辨率下的衍射结果,该晶体属于空间群P2(1),晶胞参数为a = 50.79、b = 48.79、c = 66.87 Å,β = 99.31°。初步分析表明,不对称单元中有一个几丁质酶分子,溶剂含量为43.4%。

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