Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe-0614 from Caldicellulosiruptor bescii

Hiroshi Yokoyama, Takahiro Yamashita, Naoki Horikoshi, Hitoshi Kurumizaka, Wataru Kagawa

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)438-440
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number4
DOIs
Publication statusPublished - 2013 Apr

Keywords

  • Caldicellulosiruptor bescii
  • cellulose
  • secreted proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

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