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Subcloning of a dna fragment encoding a single cohesin domain of the clostridium thermocellum cellulosome-integrating protein cipA: Purification, crystallization, and preliminary diffraction analysis of the encoded polypeptide

Abstract : An Escherichia coli clone encoding a single cohesin domain of the cellulosome-integrating protein CipA from Clostridium thermocellum was constructed, and the corresponding polypeptide was purified, treated with papain, and crystallized from a PEG 8000 solution. Crystals exhibit orthorhombic symmetry, space group P2(1)2(1)2(1), with cell dimensions a = 37.7 A, b = 80.7 A, c = 93.3 A, and four or eight molecules in the unit cell. The crystals diffract X-rays to beyond 2 A resolution and are suitable for further crystallographic studies.
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Submitted on : Tuesday, February 9, 2021 - 6:41:29 PM
Last modification on : Friday, April 2, 2021 - 11:36:00 AM

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Pierre Béguin, Odette Raynaud, Marie-Kim Chaveroche, Abel Dridi, Pedro Alzari. Subcloning of a dna fragment encoding a single cohesin domain of the clostridium thermocellum cellulosome-integrating protein cipA: Purification, crystallization, and preliminary diffraction analysis of the encoded polypeptide. Protein Science, Wiley, 1996, 5 (6), pp.1192-1194. ⟨10.1002/pro.5560050623⟩. ⟨pasteur-03136611⟩

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