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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
Author(s) -
Béguin Pierre,
Raynaud Odette,
Chaveroche MarieKim,
Dridi Abel,
Alzari Pedro M.
Publication year - 1996
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560050623
Subject(s) - clostridium thermocellum , cellulosome , pyrococcus furiosus , chemistry , cohesin , escherichia coli , crystallography , biochemistry , molecular replacement , bacillus circulans , subcloning , dna , protein structure , chromatin , gene , archaea , enzyme , cellulose , cellulase
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.