Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data

A new experimental strategy is described for obtaining time-resolved protein structural changes using monochromatic X-ray crystallographic data. The method is based on time-dependent linear interpolation of observed intensity variations during conventional X-ray diffraction data collection. The method benefits from high data redundancy. Although the method was developed to examine time-dependent X-ray-induced crystal decay, it is potentially applicable to a variety of time-dependent crystallographic studies, including structural determination of chemical intermediates in enzyme reactions and X-ray-induced unfolding of proteins with multiple disulfide bonds.