Crystallization and preliminary crystallographic analysis of the glycoside hydrolase family 115 α-glucuronidase from Streptomyces pristinaespiralis

链霉菌(Streptomyces pristinaespiralis)糖苷水解酶115家族α-葡糖醛酸酶的结晶及初步晶体学分析

阅读:1

Abstract

α-Glucuronidase from Streptomyces pristinaespiralis (SpGlcA115A) is composed of a single-chain peptide containing a catalytic domain belonging to glycosyl hydrolase family 115, a novel family of hemicellulolytic α-glucuronidases. The enzyme catalyzes the hydrolysis of α-linked 4-O-methylglucuronosyl and glucuronosyl residues from both polymeric xylans and oligosaccharides. SpGlcA115A was crystallized at 293 K using the sitting-drop vapour-diffusion method. The crystals belonged to space group R3 and diffracted to a resolution of 1.9 Å.

特别声明

1、本页面内容包含部分的内容是基于公开信息的合理引用;引用内容仅为补充信息,不代表本站立场。

2、若认为本页面引用内容涉及侵权,请及时与本站联系,我们将第一时间处理。

3、其他媒体/个人如需使用本页面原创内容,需注明“来源:[生知库]”并获得授权;使用引用内容的,需自行联系原作者获得许可。

4、投稿及合作请联系:info@biocloudy.com。