Crystallization and preliminary X-ray analysis of a cohesin-like module from AF2375 of the archaeon Archaeoglobus fulgidus

A cohesin-like module from the hyperthermophilic archaeon A. fulgidus was cloned, expressed, purified and crystallized. X-ray diffraction data were collected to 1.82 Å resolution. A cohesin-like module of 160 amino-acid residues from the hypothetical protein AF2375 of the noncellulolytic, hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus was cloned, expressed, purified, crystallized and subjected to X-ray structural study in order to compare its structure with those of cellulolytic cohesins. The crystals had cubic symmetry, with unit-cell parameters a = b = c = 101.75 Å in space group P4₃32, and diffracted to 1.82 Å resolution. The asymmetric unit contained a single cohesin molecule. A model assembled from six cohesin structures of very low sequence identity to the cohesin-like module was used in molecular-replacement attempts, producing a marginal solution