Open AccessCrystallization and preliminary X‐ray analysis of Acetivibrio cellulolyticus cellulosomal type II cohesin module: two versions having different linker lengths
Author(s) -
Noach Ilit,
Alber Orly,
Bayer Edward A.,
Lamed Raphael,
LevyAssaraf Maly,
Shimon Linda J. W.,
Frolow Felix
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107066821
Subject(s) - linker , crystallography , cohesin , orthorhombic crystal system , residue (chemistry) , crystallization , chemistry , stereochemistry , crystal structure , biochemistry , dna , chromatin , organic chemistry , computer science , operating system
The second type II cohesin module of the cellulosomal scaffoldin polypeptide ScaB from Acetivibrio cellulolyticus (CohB2) was cloned into two constructs: one containing a short (five‐residue) C‐terminal linker (CohB2_S) and the second incorporating the full native 45‐residue linker (CohB2_L). Both constructs encode proteins that also include the full native six‐residue N‐terminal linker. The CohB2_S and CohB2_L proteins were expressed, purified and crystallized in the orthorhombic crystal system, but with different unit cells and symmetries: space group P 2 1 2 1 2 1 with unit‐cell parameters a = 90.36, b = 68.65, c = 111.29 Å for CohB2_S and space group P 2 1 2 1 2 with unit‐cell parameters a = 68.76, b = 159.22, c = 44.21 Å for CohB2_L. The crystals diffracted to 2.0 and 2.9 Å resolution, respectively. The asymmetric unit of CohB2_S contains three cohesin molecules, while that of CohB2_L contains two molecules.