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Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe_0614 from Caldicellulosiruptor bescii.

ABSTRACT: 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 P2(1), with unit-cell parameters a = 48.4, b = 42.2, c = 97.8 Å, ? = 96.1°, and diffracted to 2.7 Å resolution using synchrotron radiation.

SUBMITTER: Yokoyama H

PROVIDER: S-EPMC3614173 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe_0614 from Caldicellulosiruptor bescii.

Yokoyama Hiroshi H Yamashita Takahiro T Horikoshi Naoki N Kurumizaka Hitoshi H Kagawa Wataru W

Acta crystallographica. Section F, Structural biology and crystallization communications 20130328 Pt 4

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 P2(1), with unit-cell parameters a = 48.4, b = 42.2, c = 97.8 Å, β = 96.1°, and diffracted to 2.7 Å reso ...[more]

PMID: 23545654

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