High-Level Bacterial Expression and Purification of Apicomplexan Micronemal Proteins for Structural Studies

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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.





Keywords: cysteine-rich proteins; micronemal proteins; nmr; toxoplasma gondii; x-ray crystallography

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986607780782876

Publication date: May 1, 2007

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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