Open AccessCrystallization and preliminary X‐ray analysis of a cohesin‐like module from AF2375 of the archaeon Archaeoglobus fulgidus
Author(s) -
VoronovGoldman Milana,
Noach Ilit,
Lamed Raphael,
Shimon Linda J. W.,
Borovok Ilya,
Bayer Edward A.,
Frolow Felix
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109002887
Subject(s) - cohesin , crystallography , protein data bank (rcsb pdb) , crystallization , chemistry , biochemistry , gene , chromosome , organic chemistry
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 P 4 3 32, 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.