How do you deal with commonly encountered problems and bottlenecks that occur when trying to express and purify membrane proteins (MPs) for structural biology? Current Protocols (www.currentprotocols.com) and The Protein Society (www.proteinsociety.org) are pleased to present a free 1-hour webinar by two leaders in MP production: James Love, Head of Research for the New York Consortium on Membrane Protein Structure, will speak on challenges and solutions for working with MPs in E. coli, and Mark Dumont from the will discuss the same topics for yeast systems. Plus, Drs. Love and Dumont will answer your questions live!
- Advantages and disadvantages of yeast and E. coli expression systems
- Rapid high-throughput cloning, expression and purification procedures
- Vectors and tags
- Maximizing expression levels
- Cell lysis
- Protein stability and minimizing proteolysis
- Detergent selection
James Love is Head of Research for The New York Consortium on Membrane Protein Structure (NYCOMPS), one of nine specialized centers focusing on MPs as part of the Protein Structure Initiative: Biology. Dr Love has published on high-throughput methodologies developed specifically for integral MPs, which have been used to process more than 5,000 membrane proteins. With this work, NYCOMPS has solved many exciting membrane protein structures.
Mark Dumont is a Professor of Biochemistry and Biophysics at the University of Rochester Medical School. One of the Principal Investigators of the Membrane Protein Structural Biology Consortium, he has been involved in expression and purification of MPs as part of the Center for High Throughput Structural Biology, and the project for Structural Genomics of Pathogenic Protozoa. His work on MPs in yeast has spanned individual targets to genome-wide studies.
Who Should Attend:
Researchers who need to produce MPs for functional or structural studies (e.g., activity assays or crystallization).