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

Milana Voronov-Goldman, Ilit Noach, Raphael Lamed, Linda J.W. Shimon, Ilya Borovok, Edward A. Bayer, Felix Frolow

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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 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.

Original languageEnglish
Pages (from-to)275-278
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number3
DOIs
StatePublished - 2009

Keywords

  • Archaeal proteins
  • Noncellulosomal cohesin

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