Research Description 

We are interested in understanding the physical basis of enzyme catalysis and protein signaling using time-resolved X-ray crystallography and other biophysical approaches. The advent of X-ray free electron laser (XFEL) sources that produce brief pulses of exceptionally bright X-rays now permits detailed structural characterization of biochemical phenomena at multiple timepoints after perturbation. With these time-resolved “movies” of proteins in action, we investigate the non-equilibrium structural biology of several systems, including cysteine-dependent enzymes that form mandatory covalent reaction intermediates, proteins involved in antibiotic synthesis and destruction, and proteins that are important in redox biochemistry. We are also interested in extending these new structural biology methods to synchrotron applications, which will broaden experimental access to the emerging field of non-equilibrium structural biology.