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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2(64), p. 77-80, 2008

DOI: 10.1107/s1744309107067437

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Preliminary X-ray characterization of a novel type of anchoring cohesin from the cellulosome ofRuminococcus flavefaciens

Journal article published in 2008 by Orly Alber, Ilit Noach, Raphael Lamed, Linda J. W. Shimon ORCID, Edward A. Bayer, Felix Frolow
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

Ruminococcus flavefaciens is an anaerobic bacterium that resides in the gastrointestinal tract of ruminants. It produces a highly organized multi-enzyme cellulosome complex that plays a key role in the degradation of plant cell walls. ScaE is one of the critical structural components of its cellulosome that serves to anchor the complex to the cell wall. The seleno-L-methionine-labelled derivative of the ScaE cohesin module has been cloned, expressed, purified and crystallized. The crystals belong to space group C2, with unit-cell parameters a = 155.6, b = 69.3, c = 93.0 A, beta = 123.4 degrees, and contain four molecules in the asymmetric unit. Diffraction data were phased to 1.95 A using the anomalous signal from the Se atoms.