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

研究成果: Article査読

4 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)438-440
ページ数3
ジャーナルActa Crystallographica Section F: Structural Biology and Crystallization Communications
69
4
DOI
出版ステータスPublished - 2013 4

ASJC Scopus subject areas

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

フィンガープリント 「Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe-0614 from Caldicellulosiruptor bescii」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル