Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 61, Issue -, Pages 46-48Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309104025837
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The high-affinity calcium-mediated type II cohesin-dockerin interaction is responsible for the attachment of the multi-enzyme cellulose-degrading complex, termed the cellulosome, to the cell surface of the thermophilic anaerobe Clostridium thermocellum. A trimodular 40 kDa complex comprising the SdbA type II cohesin and the the CipA type II dockerin-X module modular pair from the cellulosome of C. thermocellum has been crystallized. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 45.21, b = 52.34, c = 154.69 angstrom. The asymmetric unit contains one molecule of the protein complex and native and selenomethionine-derivative crystals diffracted to 2.1 and 2.0 angstrom, respectively.
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