title: Crystallization and preliminary X-ray diffraction data of alpha-galactosidase from Saccharomyces cerevisiae.
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.
authors.affiliation: Departamento de Bioloxía Celular e Molecular, Facultade de Ciencias, Universidade da Coruña, Campus da Zapateira, s/n 15071 A Coruña, Spain.
authors.forename: Rafael
authors.initials: R
authors.lastname: Fernández-Leiro
authors.forename: Angel
authors.initials: A
authors.lastname: Pereira-Rodríguez
authors.forename: M Esperanza
authors.initials: ME
authors.lastname: Cerdán
authors.forename: Manuel
authors.initials: M
authors.lastname: Becerra
authors.forename: Juliana
authors.initials: J
authors.lastname: Sanz-Aparicio
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D000519:alpha-Galactosidase / Q000737:chemistry*
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D000519:alpha-Galactosidase