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Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of Paenibacillus barcinonensis xylanase 10C containing the CBM22-1-CBM22-2 tandem
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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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SAINZ POLO, M. a., GONZÁLEZ NAVARRO, Beatriz, PASTOR BLASCO, Francisco i. javier, SANZ APARICIO, J.. Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of Paenibacillus barcinonensis xylanase 10C containing the CBM22-1-CBM22-2 tandem. _Acta Crystallographica Section F: Structural Biology and Crystallization Communications_. 2015. Vol. 71, núm. 2, pàgs. 136-140. [consulta: 25 de febrer de 2026]. ISSN: 1744-3091. [Disponible a: https://hdl.handle.net/2445/62364]