Center for Biomolecular Structure Lecture Series

Diffraction-based structural biology methods are a fundamental tool for structural science, accounting for close to 85% of all macromolecular structures deposited to the Protein Data Bank. Recent advances in structural biology methods, from synchrotron, electron diffraction, and XFELs to computational advances and CryoEM, have opened the door to the investigation of more challenging target samples. This talk will highlight several research projects in the Bowman Lab on metalloprotein biology and the methods available to discover how structure contributes to their unique chemistry. Metals in proteins are ubiquitous (involving up to 50% of the proteome) and involved in many of the reactions that define life – transfer of energy, photosynthesis, metabolism, oxygen shuttling, and much more. In structural work, X-ray and electron sources used in diffraction and CryoEM studies can cause changes in oxidation state and radiation damage, obscuring the true nature of the role of the metal in the protein. We are working to make use of multiple methods, including spectroscopy coupled to diffraction data collection and specialized fixed-target platforms, to probe metalloprotein biology. This suite of approaches facilitates examination of protein structure and opens paths to further studies of protein dynamics and motion.