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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.

SUBMITTER: Jindou S

PROVIDER: S-EPMC2344089 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature

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

Jindou Sadanari S Petkun Svetlana S Shimon Linda L Bayer Edward A EA Lamed Raphael R Frolow Felix F

Acta crystallographica. Section F, Structural biology and crystallization communications 20071121 Pt 12

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 ID ...[more]

PMID: 18084089

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