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酿酒酵母α-半乳糖苷酶的结晶及初步X射线衍射数据

Crystallization and preliminary X-ray diffraction data of alpha-galactosidase from Saccharomyces cerevisiae.

作者信息

Fernández-Leiro Rafael, Pereira-Rodríguez Angel, Cerdán M Esperanza, Becerra Manuel, Sanz-Aparicio Juliana

机构信息

Departamento de Bioloxía Celular e Molecular, Facultade de Ciencias, Universidade da Coruña, Campus da Zapateira, s/n 15071 A Coruña, Spain.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):44-7. doi: 10.1107/S1744309109047794. Epub 2009 Dec 25.

Abstract

Saccharomyces cerevisiae alpha-galactosidase is a highly glycosylated extracellular protein that catalyzes the hydrolysis of alpha-galactosidic linkages in various glucids. Its enzymatic activity is of interest in many food-related industries and has biotechnological applications. Glycosylated and in vitro deglycosylated protein samples were both assayed for crystallization, but only the latter gave good-quality crystals that were suitable for X-ray crystallography. The crystals belonged to space group P42(1)2, with unit-cell parameters a = b = 101.24, c = 111.52 A. A complete diffraction data set was collected to 1.95 A resolution using a synchrotron source.

摘要

酿酒酵母α-半乳糖苷酶是一种高度糖基化的细胞外蛋白,可催化各种糖类中α-半乳糖苷键的水解。其酶活性在许多食品相关行业中备受关注,并具有生物技术应用。对糖基化和体外去糖基化的蛋白质样品都进行了结晶检测,但只有后者得到了适合X射线晶体学分析的高质量晶体。这些晶体属于空间群P42(1)2,晶胞参数a = b = 101.24,c = 111.52 Å。使用同步辐射源收集了完整的衍射数据集,分辨率达到1.95 Å。

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