High-resolution structures from X-ray crystallography , Nuclear Magnetic Resonance (NMR) , and cryo-EM have established a foundation for the molecular understanding of protein, RNA, DNA, and their cofactors. However, static structures do not provide a complete picture of protein function, but an ensemble might provide a clearer bridge. Information about states beyond a single structure is critical to understand protein stability , ligand-bound states and affinities , and how different mutations impact function . Indeed, it has been observed that crystal structures of the same protein families are too similar to explain the difference in their measured physiological parameters .