Our research aims to understand how protein structural dynamics govern biological function. We investigate, with atomic spatial and temporal resolution, the conformational changes that drive enzyme catalysis, electron transfer, allosteric regulation, and molecular recognition. Understanding these dynamic processes is essential for deciphering the molecular mechanisms underlying life and for enabling the development of innovative therapeutic strategies.

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To address these questions, we combine state-of-the-art experimental and computational approaches. Our work integrates room-temperature serial crystallography and time-resolved crystallography at synchrotrons and X-ray free-electron lasers (XFELs), enabling the visualization of biomolecular processes across an exceptionally broad temporal range, from ultrafast femtosecond events to reactions occurring over seconds. These techniques are complemented by biochemistry, rapid kinetics, spectroscopy, and molecular dynamics simulations, allowing us to characterize transient functional states that remain inaccessible to conventional structural methods.

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Our research focuses primarily on enzymes and other biomolecular systems of biomedical relevance, exploring how atomic motions and conformational fluctuations regulate activity, cooperativity, and reaction mechanisms. In parallel, we develop innovative methodologies and instrumentation to advance serial crystallography, improving experimental efficiency, reducing sample consumption, and expanding the capabilities of time-resolved structural studies.

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Our long-term goal is to establish a dynamic view of biomolecular function by integrating structure, motion, and mechanism within a unified framework. Through this approach, we seek to advance the frontiers of structural biology while providing fundamental insights that support the rational design of next-generation therapeutics and biocatalysts.