Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.


Journal article


Protein Pept Lett

Publication Date





411 - 415


Animals, Cell Adhesion Molecules, Chromatography, Gel, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Nuclear Magnetic Resonance, Biomolecular, Protozoan Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Toxoplasma