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

Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1529-31. doi: 10.1107/S2053230X14019815. Epub 2014 Oct 25.

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.

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

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aspergillus niger / enzymology*
  • Aspergillus niger / genetics
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Crystallization
  • Databases, Genetic
  • Molecular Sequence Data
  • X-Ray Diffraction
  • beta-Galactosidase / chemistry*
  • beta-Galactosidase / genetics

Substances

  • Bacterial Proteins
  • beta-Galactosidase