My research activity is focused on the understanding of structure-function-dynamics relationships in proteins and on the coupling between protein and solvent dynamics. The biophysical techniques employed include neutron scattering and temperature-controlled X-ray cryo-crystallography. Elastic incoherent neutron scattering allows the determination of atomic motions on the ns-ps time scale averaged over the entire protein. Temperature-controlled X-ray cryo-crystallography, on the other hand, informs about spatially-resolved flexibility of protein structures. In this context, intense synchrotron radiation has been discovered to produce specific chemical damage to crystalline proteins that proves to be a valuable tool to monitor structural flexibility. Dynamical changes of the solvent in protein crystals or in stacks of biological membranes influence protein dynamics and are studied by X-ray and neutron diffraction and microspectrophotometry. The ensemble of dynamical information thus gathered provides the groundwork for trapping and structural characterization of intermediate states cholinesterases by combining cryo-photolysis of 'caged compounds' and temperature-controlled protein X-ray crystallography.