Crystallization and preliminary X-ray diffraction analysis of the invertase from Saccharomyces cerevisiae

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1538-41. doi: 10.1107/S1744309112044417. Epub 2012 Nov 19.

Abstract

Saccharomyces cerevisiae invertase (ScInv) is an enzyme encoded by the SUC2 gene that releases β-fructose from the nonreducing termini of various β-D-fructofuranoside substrates. Its ability to produce 6-kestose by transglycosylation makes this enzyme an interesting research target for applications in industrial biotechnology. The native enzyme, which presents a high degree of oligomerization, was crystallized by vapour-diffusion methods. The crystals belonged to space group P3(1)21, with unit-cell parameters a=268.6, b=268.6, c=224.4 Å. The crystals diffracted to 3.3 Å resolution and gave complete data sets using a synchrotron X-ray source.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Trisaccharides / chemistry
  • Trisaccharides / metabolism
  • X-Ray Diffraction
  • beta-Fructofuranosidase / chemistry*

Substances

  • Saccharomyces cerevisiae Proteins
  • Trisaccharides
  • 6-kestose
  • SUC2 protein, S cerevisiae
  • beta-Fructofuranosidase