Our group explores how enzymes and signaling proteins work by watching them in motion. We use cutting-edge tools like time-resolved X-ray crystallography at X-ray free-electron lasers (XFELs) and synchrotrons to capture structural “snapshots” of proteins as they perform their functions. These snapshots come together as molecular movies that reveal how proteins breathe, bend, and react in real time. We are particularly fascinated by flavoenzymes, redox-active proteins, and enzymes involved in antibiotic resistance, where subtle shifts in shape or charge can determine whether a reaction proceeds—or fails. By combining XFEL experiments, room-temperature crystallography, and computational modeling, we uncover the hidden dynamics that underlie enzyme catalysis, allostery, and redox communication. Beyond answering fundamental questions about how proteins work, we are also developing new experimental strategies that bring the power of time-resolved structural biology to synchrotron facilities, making this exciting field more widely accessible. Ultimately, our goal is to connect structure, dynamics, and function to understand—and eventually control—the remarkable chemistry of life in motion.