Wednesday, June 17, 2009, 4:00 pm — John Dunn Seminar Room, Bldg. 463
X-ray crystallography is a powerful tool to probe biological structure and function. However, very rapid changes can occur in crystals during X-ray data collection at electrophilic sites such as metals and cofactors. These can include changes in redox state, bond breakage, and loss of ligands. Single crystal spectroscopy provides a sensitive probe of these X-ray-induced changes. I will present examples of the use of single-crystal UV-Visible spectroscopy to follow changes in cofactor redox state during X-ray exposure, and to show how this information can be used to define data-collection strategies to obtain undamaged structures. I will also discuss new developments in the instrumentation available for single-crystal spectroscopy at synchrotron sources which are expanding the range of accessible spectroscopic techniques to study both radiation damage and biological function.
Hosted by: Allen Orville
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