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

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

Acta crystallographica. Section F, Structural biology and crystallization communications (2012-11-30)
M Angela Sainz-Polo, Alvaro Lafraya, Aitana Polo, Julia Marín-Navarro, Julio Polaina, Julia Sanz-Aparicio
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Invertase Glycoprotein Standard, BioReagent, from Saccharomyces cerevisiae, for proteomics
Supelco
Invertase from baker′s yeast (S. cerevisiae), 200-300 units/mg solid
Sigma-Aldrich
Invertase from Candida utilis, Grade X, ≥300 units/mg solid
Sigma-Aldrich
Invertase from baker′s yeast (S. cerevisiae), Grade VII, ≥300 units/mg solid