Cloning, expression, purification, crystallization and initial crystallographic analysis of the preprotein translocation ATPase SecA from Thermus thermophilus

Marina N. Vassylyeva, Hiroyuki Mori, Tomoya Tsukazaki, Shigeyuki Yokoyama, Tahir H Tahirov, Koreaki Ito, Dmitry G. Vassylyev

Research output: Contribution to journalArticle

2 Scopus citations


The Thermus thermophilus gene encoding the preprotein translocation ATPase SecA was cloned and expressed and the purified protein was crystallized by the hanging-drop vapour-diffusion technique in two different space groups P3 1(2)21 (a = b = 168.6, c = 149.8 Å) and P61(5)22 (a = b = 130.9, c = 564.6 Å). The crystals, improved by macroseeding, diffracted to beyond 2.8 and 3.5 Å resolution for the trigonal and hexagonal crystal forms, respectively. Structure determination using the multiple isomorphous replacement method is in progress.

Original languageEnglish (US)
Pages (from-to)909-912
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number9
Publication statusPublished - Sep 1 2006


ASJC Scopus subject areas

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

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