Sainz Polo, M. A.González Navarro, BeatrizPastor Blasco, Francisco I. JavierSanz Aparicio, J.2015-02-042015-02-042015-021744-3091https://hdl.handle.net/2445/62364A 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 affinity6 p.application/pdfeng(c) International Union of Crystallography, 2015Enzims microbiansBiopolímersBiotecnologiaMicrobial enzymesBiopolymersBiotechnologyinfo:eu-repo/semantics/article6463272015-02-04info:eu-repo/semantics/openAccess25664784