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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.

Type

Journal article

Journal

Protein Pept Lett

Publication Date

2007

Volume

14

Pages

411 - 415

Keywords

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