Overproduction, purification, crystallization and preliminary X-ray characterization of a novel carbohydrate-binding module of endoglucanase Cel5A from Eubacterium cellulosolvens

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

The anaerobic cellulolytic rumen bacterium Eubacterium cellulosolvens produces a large array of cellulases and hemicellulases that are responsible for the hydrolysis of plant cell-wall polysaccharides. One of these enzymes, endoglucanase Cel5A, comprises two tandemly repeated novel carbohydrate-binding modules (CBMs) and two catalytic domains belonging to glycoside hydrolase family 5 joined by flexible linker sequences. The novel CBM located at the N-terminus of the endoglucanase has been crystallized. The crystals belonged to the hexagonal space group P6(1)22 and contained a single molecule in the asymmetric unit. The structure of the l-selenomethionine derivative has been solved by a MAD experiment on crystals that diffracted to 1.75 A resolution.
Original languageUnknown
Pages (from-to)491-493
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue numberNA
DOIs
Publication statusPublished - 1 Jan 2011

Cite this