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crystallization communications
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 (PDB entries 1anu
, 1aoh
, 1g1k
, 1qzn
, 1zv9
and 1tyj
) of very low sequence identity to the cohesin-like module was used in molecular-replacement attempts, producing a marginal solution.