TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe-0614 from Caldicellulosiruptor bescii
AU - Yokoyama, Hiroshi
AU - Yamashita, Takahiro
AU - Horikoshi, Naoki
AU - Kurumizaka, Hitoshi
AU - Kagawa, Wataru
PY - 2013/4
Y1 - 2013/4
N2 - The Athe-0614 protein is a component of the extracellular proteins secreted by the anaerobic, extremely thermophilic and cellulolytic bacterium Caldicellulosiruptor bescii. The recombinant protein was expressed in Escherichia coli, purified to near-homogeneity and crystallized using polyethylene glycol 2000 monomethyl ether as a precipitant. The crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 48.4, b = 42.2, c = 97.8 Å, β = 96.1°, and diffracted to 2.7 Å resolution using synchrotron radiation.
AB - The Athe-0614 protein is a component of the extracellular proteins secreted by the anaerobic, extremely thermophilic and cellulolytic bacterium Caldicellulosiruptor bescii. The recombinant protein was expressed in Escherichia coli, purified to near-homogeneity and crystallized using polyethylene glycol 2000 monomethyl ether as a precipitant. The crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 48.4, b = 42.2, c = 97.8 Å, β = 96.1°, and diffracted to 2.7 Å resolution using synchrotron radiation.
KW - Caldicellulosiruptor bescii
KW - cellulose
KW - secreted proteins
UR - http://www.scopus.com/inward/record.url?scp=84875848600&partnerID=8YFLogxK
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U2 - 10.1107/S174430911300554X
DO - 10.1107/S174430911300554X
M3 - Article
C2 - 23545654
AN - SCOPUS:84875848600
VL - 69
SP - 438
EP - 440
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
SN - 1744-3091
IS - 4
ER -