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Crystallization and preliminary X‐ray diffraction analysis of the secreted protein Athe_0614 from Caldicellulosiruptor bescii
Author(s) -
Yokoyama Hiroshi,
Yamashita Takahiro,
Horikoshi Naoki,
Kurumizaka Hitoshi,
Kagawa Wataru
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911300554x
Subject(s) - chemistry
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 P 2 1 , 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.

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