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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Adhesion Molecules / biosynthesis
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Cell Adhesion Molecules / isolation & purification*
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Chromatography, Gel
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Cloning, Molecular / methods*
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / metabolism
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Nuclear Magnetic Resonance, Biomolecular
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Protozoan Proteins / biosynthesis
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Protozoan Proteins / isolation & purification*
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Toxoplasma / chemistry*
Substances
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Cell Adhesion Molecules
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MIC1 protein, Toxoplasma gondii
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Protozoan Proteins