Abstract The central goal of this project is to understand how protein motion gives rise to function. However, visualizing proteins in motion is a problem that is inherently difficult in structural biology as it involves signals from many conformations. To tackle this challenge, we take an interdisciplinary approach. We apply our understanding of the theory of scattering-based structural methods to develop new computational methods for processing and interpretating data representing conformational disorder. We have developed methods to extract dynamic infor- mation from protein crystals that have the potential to animate crystal structures, and we have mapped the structural interconversions of allosteric and flexible enzymes. In the coming years, we will continue to tackle fundamental questions about the molecular mechanisms of protein allostery and catalysis, and to do so, we will expand the scope of our work by integrating cryo-electron microscopy (cryo-EM) with advanced X-ray methods. Our goals are to: capture correlated motions in allosteric networks, apply our expertise with mathematical de- composition to the problem of conformational heterogeneity, and (3) probe protein motions that control catalysis.