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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 3(65), p. 275-278, 2009

DOI: 10.1107/s1744309109002887

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

Journal article published in 2009 by Milana Voronov-Goldman, Ilit Noach, Raphael Lamed, Linda J. W. Shimon ORCID, Ilya Borovok ORCID, Edward A. Bayer, Felix Frolow
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This paper is available in a repository.

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Abstract

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 A in space group P4(3)32, and diffracted to 1.82 A 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.