TY - JOUR
T1 - Crystallization and preliminary diffraction studies of CBM3b of cellobiohydrolase 9A from Clostridium thermocellum
AU - Jindou, Sadanari
AU - Petkun, Svetlana
AU - Shimon, Linda
AU - Bayer, Edward A.
AU - Lamed, Raphael
AU - Frolow, Felix
PY - 2007/11/30
Y1 - 2007/11/30
N2 - Family 3 carbohydrate-binding modules (CBM3s) are associated with the scaffoldin subunit of the multi-enzyme cellulosome complex and with the family 9 glycoside hydrolases, which are multimodular enzymes that act on plant cell-wall polysaccharides, notably cellulose. Here, the crystallization of CBM3b from cellobiohydrolase 9A is reported. The crystals are tetragonal and belong to space group P41 or P43. X-ray diffraction data for CBM3b have been collected to 2.68 Å resolution on beamline ID14-4 at the ESRF.
AB - Family 3 carbohydrate-binding modules (CBM3s) are associated with the scaffoldin subunit of the multi-enzyme cellulosome complex and with the family 9 glycoside hydrolases, which are multimodular enzymes that act on plant cell-wall polysaccharides, notably cellulose. Here, the crystallization of CBM3b from cellobiohydrolase 9A is reported. The crystals are tetragonal and belong to space group P41 or P43. X-ray diffraction data for CBM3b have been collected to 2.68 Å resolution on beamline ID14-4 at the ESRF.
KW - Family 3 carbohydrate-binding modules
UR - http://www.scopus.com/inward/record.url?scp=36849077668&partnerID=8YFLogxK
U2 - 10.1107/S1744309107054644
DO - 10.1107/S1744309107054644
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C2 - 18084089
AN - SCOPUS:36849077668
SN - 1744-3091
VL - 63
SP - 1044
EP - 1047
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 12
ER -