Protein Pept Lett. 2007;14(5):411-5.
High-level bacterial expression and purification of apicomplexan micronemal proteins for structural studies
Saouros S, Blumenschein TM, Sawmynaden K, Marchant J, Koutroukides T, Liu B, Simpson P, Carpenter EP, Matthews SJ.
Department of Biological Sciences, Division of Molecular Biosciences, Centre for Structural Biology, Imperial College London, South Kensington, London SW7 2AZ, UK. email@example.com.
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.
PMID: 17584164 [PubMed - in process]