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: toxoplasma gondii, micronemal proteins, cysteine-rich proteins, nmr, x-ray crystallography
Protein & Peptide Letters
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.
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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
DOI https://dx.doi.org/10.2174/092986607780782876 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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