Conformational stabilization and crystallization of the SecA translocation ATPase from Bacillus subtilis

S. Weinkauf, J. F. Hunt, J. Scheuring, L. Henry, J. Fak, D. B. Oliver, J. Deisenhofer

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

The SecA translocation ATPase acts as a molecular motor which drives the translocation of proteins through bacterial membranes. In doing so it undergoes large conformational changes and this flexibility may hinder crystallization of the protein. Stabilization of this protein's conformation and its crystallization have been achieved using high glycerol concentrations.

Original languageEnglish (US)
Pages (from-to)559-565
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number4
DOIs
StatePublished - 2001

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ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

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