Literature DB >> 20057068

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

Rafael Fernández-Leiro1, Angel Pereira-Rodríguez, M Esperanza Cerdán, Manuel Becerra, Juliana Sanz-Aparicio.   

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.

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Year:  2009        PMID: 20057068      PMCID: PMC2805534          DOI: 10.1107/S1744309109047794

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  13 in total

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  2 in total

1.  Structural analysis of Saccharomyces cerevisiae alpha-galactosidase and its complexes with natural substrates reveals new insights into substrate specificity of GH27 glycosidases.

Authors:  Rafael Fernández-Leiro; Angel Pereira-Rodríguez; M Esperanza Cerdán; Manuel Becerra; Juliana Sanz-Aparicio
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2.  Optimization of Saccharomyces cerevisiae α-galactosidase production and application in the degradation of raffinose family oligosaccharides.

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  2 in total

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