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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, B.
Pastor Blasco, Francisco I. Javier
Sanz Aparicio, J.
Keywords: Enzims microbians
Microbial enzymes
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
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It is part of: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2015, vol. 71, num. 2, p. 136-140
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ISSN: 1744-3091
Appears in Collections:Articles publicats en revistes (Genètica, Microbiologia i Estadística)

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