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

Journal article

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.

Authors: Saouros, S; Blumenschein, T; Sawmynaden, K; Marchant, J; Koutroukides, T

• Publication status: Published
• Journal: Protein and peptide letters
• Volume: 14
• Issue: 5
• Pages: 411-415
• Publication date: 2007-01-01
• DOI: 10.2174/092986607780782876
• EISSN: 1875-5305
• ISSN: 0929-8665
• Language: English
• Keywords: Toxoplasma; Animals; Escherichia coli; Chromatography, Gel; Cell Adhesion Molecules; Nuclear Magnetic Resonance, Biomolecular; Protozoan Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Electrophoresis, Polyacrylamide Gel; Cloning, Molecular