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Overproduction, purification, crystallization and preliminary X-ray characterization of the C-terminal family 65 carbohydrate-binding module (CBM65B) of endoglucanase Cel5A from Eubacterium cellulosolvens

Lookup NU author(s): Dr Max Temple, Emeritus Professor Harry Gilbert


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The rumen anaerobic cellulolytic bacterium Eubacterium cellulosolvens produces a large range of cellulases and hemicellulases responsible for the efficient hydrolysis of plant cell wall polysaccharides. One of these enzymes, endoglucanase Cel5A, comprises a tandemly repeated carbohydrate-binding module (CBM65) fused to a glycoside hydrolase family 5 (Cel5A) catalytic domain, joined by flexible linker sequences. The second carbohydrate-binding module located at the C-terminus side of the endoglucanase (CBM65B) has been co-crystallized with either cellohexaose or xyloglucan heptasaccharide. The crystals belong to the hexagonal space group P6(5) and tetragonal space group P4(3)2(1)2, containing a single molecule in the asymmetric unit. The structures of CBM65B have been solved by molecular replacement.

Publication metadata

Author(s): Venditto I, Basle A, Luis AS, Temple MJ, Ferreira LMA, Fontes CMGA, Gilbert HJ, Najmudin S

Publication type: Article

Publication status: Published

Journal: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

Year: 2013

Volume: 69

Pages: 191-194

Print publication date: 01/02/2013

ISSN (print): 1744-3091

ISSN (electronic):

Publisher: Wiley-Blackwell Publishing, Inc.


DOI: 10.1107/S1744309113001620


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Funder referenceFunder name
263916European Union
PTDC/BIA-PRO/103980/2008Fundacao para a Ciencia e a Tecnologia (Lisbon, Portugal)
PTDC/QUI-BIO/100359/2008Fundacao para a Ciencia e a Tecnologia (Lisbon, Portugal)