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Crystallization and preliminary diffraction studies of CBM3b of cellobiohydrolase 9A from Clostridium thermocellum

Journal Article · · Acta Crystallographica. Section F
 [1];  [1];  [2];  [3]; ;  [1]
  1. Department of Molecular Microbiology and Biotechnology, Tel Aviv University 69978 (Israel)
  2. Department of Chemical Research Support, The Weizmann Institute of Science, Rehovot 76100 (Israel)
  3. Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100 (Israel)
The cloning, expression, purification and crystallization of the CBM3b module of cellobiohydrolase 9A from C. thermocellum is described. The crystals diffract to 2.68 Å. Family 3 carbohydrate-binding modules (CBM3s) are associated with the scaffoldin subunit of the multi-enzyme cellulosome complex and with the family 9 glycoside hydrolases, which are multimodular enzymes that act on plant cell-wall polysaccharides, notably cellulose. Here, the crystallization of CBM3b from cellobiohydrolase 9A is reported. The crystals are tetragonal and belong to space group P4{sub 1} or P4{sub 3}. X-ray diffraction data for CBM3b have been collected to 2.68 Å resolution on beamline ID14-4 at the ESRF.
OSTI ID:
22360435
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 12 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English