Expression, purification and crystallization of a cohesin domain from the cellulosome of Clostridium thermocellum

Sima Yaron, Linda J.W. Shimon, Felix Frolow, Raphael Lamed, Ely Morag, Yuval Shoham, Edward A. Bayer*

*Corresponding author for this work

Research output: Contribution to journalConference articlepeer-review

12 Scopus citations


The cellulosome of the cellulolytic bacterium, Clostridium thermocellum, is a multi-enzyme complex in which the enzymatic (cellulolytic) subunits are attached to a unique nonhydrolytic subunit called scaffoldin. The attachment is mediated by two mutually interacting domains: namely, multiple cohesin domains on the scaffoldin subunit and a dockerin domain on each of the enzymatic subunits. Knowledge of the three-dimensional structure of each of the interacting components would be critical to a better understanding of the cohesin-dockerin interaction at the molecular level. In this report, we describe the purification of one of the nine cohesin domains of the scaffoldin subunit from C. thermocellum. A DNA segment containing the cohesin 2 sequence was fused to a hexa-histidine tag, and the resultant construct was expressed in Escherichia coli. The expressed peptide was efficiently isolated by metal-chelate affinity chromatography. The purified recombinant form of the cohesin was crystallized pending determination of its structure.

Original languageEnglish
Pages (from-to)243-249
Number of pages7
JournalJournal of Biotechnology
Issue number3
StatePublished - 15 Nov 1996
EventProceedings of the 1995 Workshop on Environmental Biotechnology -
Duration: 28 Nov 199528 Nov 1995


FundersFunder number
Minerva Foundation
Israel Academy of Sciences and Humanities
Israel Science Foundation


    • Clostridium thermocellum
    • X-ray crystallography
    • cellulases
    • cellulosome
    • cohesin domain


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