title: Crystallization and preliminary diffraction studies of CBM3b of cellobiohydrolase 9A from Clostridium thermocellum.
abstract: 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(1) or P4(3). X-ray diffraction data for CBM3b have been collected to 2.68 A resolution on beamline ID14-4 at the ESRF.
authors: Department of Molecular Microbiology and Biotechnology, Tel Aviv University 69978, Israel.
authors: Sadanari
authors: S
authors: Jindou
authors: Svetlana
authors: S
authors: Petkun
authors: Linda
authors: L
authors: Shimon
authors: Edward A
authors: EA
authors: Bayer
authors: Raphael
authors: R
authors: Lamed
authors: Felix
authors: F
authors: Frolow
mesh_terms: D000595:Amino Acid Sequence; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000737:chemistry*; D043366:Cellulose 1,4-beta-Cellobiosidase / Q000737:chemistry* / Q000378:metabolism*; D048013:Acetivibrio thermocellus / Q000201:enzymology*; D017124:Conserved Sequence; D003460:Crystallization; D008969:Molecular Sequence Data; D011485:Protein Binding; D016415:Sequence Alignment; D014961:X-Ray Diffraction
chemical_list: D002241:Carbohydrates; D043366:Cellulose 1,4-beta-Cellobiosidase