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

Abstract

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
Volume62
Issue number9
DOIs
StatePublished - Sep 2006

ASJC Scopus subject areas

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

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