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

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.

SUBMITTER: Voronov-Goldman M

PROVIDER: S-EPMC2650457 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

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

Voronov-Goldman Milana M Noach Ilit I Lamed Raphael R Shimon Linda J W LJ Borovok Ilya I Bayer Edward A EA Frolow Felix F

Acta crystallographica. Section F, Structural biology and crystallization communications 20090226 Pt 3

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 cont ...[more]

PMID: 19255482

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