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Título

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

AutorSainz-Polo, M. Ángela CSIC; Lafraya Aguado, Álvaro; Polo, Aitana CSIC; Marín-Navarro, Julia; Polaina Molina, Julio CSIC ORCID; Sanz-Aparicio, J. CSIC ORCID
Palabras claveInvertases
Saccharomyces cerevisiae
Fecha de publicación25-oct-2012
EditorInternational Union of Crystallography
CitaciónActa Crystallographica Section F: Structural Biology and Crystallization Communications 68: 1538-1541 (2012)
ResumenSaccharomyces 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 P3121, with unit-cell parameters a = 268.6, b = 268.6, c = 224.4 A. The crystals diffracted to 3.3 A resolution and gave complete data sets using a synchrotron X-ray source. © 2012. © 2012 International Union of Crystallography All rights reserved.
Descripción4 pags, 4 figs
Versión del editorhttp://dx.doi.org/10.1107/S1744309112044417
URIhttp://hdl.handle.net/10261/253831
DOI10.1107/S1744309112044417
Identificadoresdoi: 10.1107/S1744309112044417
issn: 1744-3091
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