Open AccessCrystallization and preliminary X‐ray diffraction data of α‐galactosidase from Saccharomyces cerevisiae
Author(s) -
FernándezLeiro Rafael,
PereiraRodríguez Ángel,
Cerdán M. Esperanza,
Becerra Manuel,
SanzAparicio Juliana
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109047794
Subject(s) - crystallization , saccharomyces cerevisiae , hydrolysis , diffraction , crystallography , x ray crystallography , chemistry , resolution (logic) , x ray , enzyme , synchrotron , biochemistry , yeast , organic chemistry , physics , optics , computer science , artificial intelligence
Saccharomyces cerevisiae α‐galactosidase is a highly glycosylated extracellular protein that catalyzes the hydrolysis of α‐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 P 42 1 2, with unit‐cell parameters a = b = 101.24, c = 111.52 Å. A complete diffraction data set was collected to 1.95 Å resolution using a synchrotron source.