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Crystallization and preliminary X-ray diffraction data of ?-galactosidase from Aspergillus niger.

ABSTRACT: ?-Galactosidase from Aspergillus niger (An-?-Gal), belonging to the family 35 glycoside hydrolases, hydrolyzes the ?-galactosidase linkages in lactose and other galactosides. It is extensively used in industry owing to its high hydrolytic activity and safety. The enzyme has been expressed in yeasts and purified by immobilized metal-ion affinity chromatography for crystallization experiments. The recombinant An-?-Gal, deglycosylated to avoid heterogeneity of the sample, has a molecular mass of 109?kDa. Rod-shaped crystals grew using PEG 3350 as the main precipitant agent. A diffraction data set was collected to 1.8?Å resolution.

SUBMITTER: Rico-Diaz A

PROVIDER: S-EPMC4231858 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction data of β-galactosidase from Aspergillus niger.

Rico-Díaz Agustín A Vizoso Vázquez Ángel Á Cerdán M Esperanza ME Becerra Manuel M Sanz-Aparicio Julia J

Acta crystallographica. Section F, Structural biology communications 20141025 Pt 11

β-Galactosidase from Aspergillus niger (An-β-Gal), belonging to the family 35 glycoside hydrolases, hydrolyzes the β-galactosidase linkages in lactose and other galactosides. It is extensively used in industry owing to its high hydrolytic activity and safety. The enzyme has been expressed in yeasts and purified by immobilized metal-ion affinity chromatography for crystallization experiments. The recombinant An-β-Gal, deglycosylated to avoid heterogeneity of the sample, has a molecular mass of 10 ...[more]

PMID: 25372823

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