Crystal structures of protein-ligand complexes provide a detailed view of their spatial arrangement and interactions. In the case of stable, unreactive ligands, such as inhibitors or allosteric regulators, the complexes can be generated by cocrystallization or by soaking the ligand into fully grown crystals. In order to obtain highly occupied stochiometric complexes, the concentration and amount of ligand used needs to be considered. Protein complexes with reactive short-lived species that occur in chemical or binding reactions can be determined using monochromatic X-ray diffraction techniques via kinetic trapping approaches. To this end, the kinetics of the reaction has to be determined in the crystalline state and triggering methods to start the reaction need to be established. To facilitate data interpretation, the experimental conditions are usually chosen such that the peak concentration of the reactive species under investigation is maximized.