Determining atomic-level architecture of biomolecules provides us with striking three-dimensional structural representations of biological machines with exquisite detail. High resolution, undamaged structure-level information is critical to understanding the roles these molecules play in disease processes and in biological mechanisms. In the Bowman Group, our research focus is two-fold.

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• First, we are developing new methods to crystallize biomolecules, as well as to detect and handle micro- and nanocrystals, for cutting-edge structural techniques, with an ultimate goal to probe how conformational changes mediate function. The techniques we use include diffraction methods using synchrotrons, X-ray Free Electron Laser (XFEL), and cryoEM for electron diffraction.

• Second, we are investigating metalloprotein structure, function, and dynamics, using structural and spectroscopic approaches to examine the ways metals impact and modulate function of these proteins. We are working to develop spectroscopic methods for single crystals (electron paramagnetic resonance, UV-visible microspectrophotometry, and energy dispersive X-ray spectroscopy for elemental analysis) to be used in parallel with crystallography. 

 

Our long-term research aims will couple these two areas: using these new structural approaches to interrogate dynamics and conformational changes in metalloproteins.

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At the Crystallization Center, we provide high-throughput screening for biomolecules to determine initial crystallization conditions, working with scientists around the world (www.getacrystal.org).

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Software and scripting developed in the Bowman Lab are available on GitHub.