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Title: | Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of Paenibacillus barcinonensis xylanase 10C containing the CBM22-1-CBM22-2 tandem |
Author: | Sainz Polo, M. A. González Navarro, Beatriz Pastor Blasco, Francisco I. Javier Sanz Aparicio, J. |
Keywords: | Enzims microbians Biopolímers Biotecnologia Microbial enzymes Biopolymers Biotechnology |
Issue Date: | Feb-2015 |
Publisher: | International Union of Crystallography |
Abstract: | A construct containing the CBM22-1-CBM22-2 tandem forming the N-terminal domain of Paenibacillus barcinonensis xylanase 10C (Xyn10C) has been purified and crystallized. A xylan-binding function and an affinity for mixed [beta]-1,3/[beta]-1,4 glucans have previously been demonstrated for some members of the CBM22 family. The sequence of the tandem is homologous to the N-terminal domains found in several thermophilic enzymes. Crystals of this tandem were grown by the streak-seeding method after a long optimization strategy. The structure has been determined by molecular replacement to a resolution of 2.43 Å and refinement is under way. This study represents the first structure containing two contiguous CBM22 modules, which will contribute to a better understanding of the role that this multiplicity plays in fine-tuning substrate affinity |
Note: | Reproducció del document publicat a: http://dx.doi.org/10.1107/S2053230X14027496 |
It is part of: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2015, vol. 71, num. 2, p. 136-140 |
URI: | http://hdl.handle.net/2445/62364 |
Related resource: | http://dx.doi.org/10.1107/S2053230X14027496 |
ISSN: | 1744-3091 |
Appears in Collections: | Articles publicats en revistes (Genètica, Microbiologia i Estadística) |
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