High-level bacterial expression and purification of apicomplexan micronemal proteins for structural studies

  • S. Saouros
  • , T. M.A. Blumenschein
  • , K. Sawmynaden
  • , J. Marchant
  • , T. Koutroukides
  • , B. Liu
  • , P. Simpson
  • , E. P. Carpenter
  • , S. J. Matthews

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The cysteine-rich N-terminal domain of the micronemal adhesive protein MIC1 (MIC1-NT) from Toxoplasma gondii was cloned, expressed in Escherichia coli and purified. MIC1-NT is amenable to structural studies as shown by preliminary NMR and X-ray analysis. Positive results with two further micronemal proteins indicate that our strategy has wider application.

Original languageEnglish
Pages (from-to)411-415
Number of pages5
JournalProtein and Peptide Letters
Volume14
Issue number5
DOIs
StatePublished - May 2007
Externally publishedYes

Keywords

  • Cysteine-rich proteins
  • Micronemal proteins
  • NMR
  • Toxoplasma gondii
  • X-ray crystallography

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