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Título: | Crystallization and preliminary X-ray diffraction analysis of the invertase from Saccharomyces cerevisiae |
Autor: | Sainz-Polo, M. Ángela CSIC; Lafraya Aguado, Álvaro; Polo, Aitana CSIC; Marín-Navarro, Julia; Polaina Molina, Julio CSIC ORCID; Sanz-Aparicio, J. CSIC ORCID | Palabras clave: | Invertases Saccharomyces cerevisiae |
Fecha de publicación: | 25-oct-2012 | Editor: | International Union of Crystallography | Citación: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications 68: 1538-1541 (2012) | Resumen: | 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 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. | Descripción: | 4 pags, 4 figs | Versión del editor: | http://dx.doi.org/10.1107/S1744309112044417 | URI: | http://hdl.handle.net/10261/253831 | DOI: | 10.1107/S1744309112044417 | Identificadores: | doi: 10.1107/S1744309112044417 issn: 1744-3091 |
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