Literature DB >> 25372823

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

Agustín Rico-Díaz1, Ángel Vizoso Vázquez1, M Esperanza Cerdán1, Manuel Becerra1, Julia Sanz-Aparicio2.   

Abstract

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 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.

Entities:  

Keywords:  Aspergillus niger; glycosidase hydrolase family 35; β-galactosidase

Mesh:

Substances:

Year:  2014        PMID: 25372823      PMCID: PMC4231858          DOI: 10.1107/S2053230X14019815

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


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