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

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 Å, b = 80.7 Å, c = 93.3 Å, and four or eight molecules in the unit cell. The crystals diffract X‐rays to beyond 2 Å resolution and are suitable for further crystallographic studies.