All chemical and biological reactions involve atomic motion, embodied in dynamic structural changes. Identifying these changes is the goal of time-resolved crystallography. The “raw” output of a time-resolved macromolecular crystallography experiment is the time-dependent set of difference electron density maps that span the desired time range and display the time-dependent changes in density (and underlying structure) as the reaction progresses. The goal is to interpret such data in terms of a small number of crystallographically refinable, time-independent structures, each associated with a reaction intermediate; to establish the pathways and rate coefficients by which the intermediates interconvert; and thus to establish a chemical kinetic mechanism. We review briefly the various strategies that may be used to achieve this goal and concentrate on two promising advances: singular value decomposition and cluster analysis. The strategies are illustrated by using data on the photocycle of the bacterial blue light photoreceptor, photoactive yellow protein.