Crystallization and preliminary X-ray analysis of Acetivibrio cellulolyticus cellulosomal type II cohesin module: two versions having different linker lengths.
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 P2(1)2(1)2(1) with unit-cell parameters a = 90.36, b = 68.65, c = 111.29 A for CohB2_S and space group P2(1)2(1)2 with unit-cell parameters a = 68.76, b = 159.22, c = 44.21 A for CohB2_L. The crystals diffracted to 2.0 and 2.9 A resolution, respectively. The asymmetric unit of CohB2_S contains three cohesin molecules, while that of CohB2_L contains two molecules.
Noach
Ilit
I
Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel.
Alber
Orly
O
Bayer
Edward A
EA
Lamed
Raphael
R
Levy-Assaraf
Maly
M
Shimon
Linda J W
LJ
Frolow
Felix
F
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D004269:DNA, Bacterial / Q000235:genetics; D016937:Gram-Positive Endospore-Forming Rods / Q000235:genetics*; D012680:Sensitivity and Specificity
D001426:Bacterial Proteins; D002352:Carrier Proteins; D004269:DNA, Bacterial