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Torpedo AChR crystallization. Since 1996 our laboratory has screened thousands of crystallization conditions using AChR purified from T. californica and T. nobiliana. This project is done in close collaboration with the Stevens laboratory at The Scripps Research Institute (http://stevens.scripps.edu) where a joint graduate student, Guillermo Asmar, M.S. from UPR is working. This collaboration enables critical access to the Joint Center for Innovative Membrane Protein Technologies (http://jcimpt.scripps.edu), as well as other high throughput crystallization, imaging, and synchrotron beam time. During this period we have gathered an enormous amount of data and very encouraging results. Our immediate goal is to better understand the effect of lipids and detergents on AChR channel activity, and use this information to improve the quality of these AChR crystals via fine-screening to achieve higher resolution diffraction. Our immediate goal is to define which detergents are suitable for the AChR crystallization using a combination of functional and structural studies (i.e. ion channel bilayer recording, EM microscopy, dynamic light scattering (DLS), Size-exclusion chromatography (SEC) and lipid analysis). The long-term goal of these experiments is to obtain a medium-resolution (3-4 Å) structure of the Torpedo AChR.
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