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

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

Volume: 14 Issue: 5

Author(s): S. Saouros, T. M.A. Blumenschein, K. Sawmynaden, J. Marchant, T. Koutroukides, B. Liu, P. Simpson, E. P. Carpenter and S. J. Matthews

Affiliation:

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

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.

Cite this article as:

Saouros S., Blumenschein M.A. T., Sawmynaden K., Marchant J., Koutroukides T., Liu B., Simpson P., Carpenter P. E. and Matthews J. S., High-Level Bacterial Expression and Purification of Apicomplexan Micronemal Proteins for Structural Studies, Protein & Peptide Letters 2007; 14 (5) . https://dx.doi.org/10.2174/092986607780782876