Protein crystallography has been the most successful technique for determining 3D structures from protein molecules. However, the technique has several disadvantages including the need of a crystalline sample, the unavoidable radiation damage and a static, averaged on time and space, resulting model. This is particularly relevant because it has been demonstrated that proteins are dynamic entities whose catalytic properties rely remarkably in their dynamic behavior. Several strategies (for example chemical and physical trap) have been developed in order to extract this dynamical information from protein crystals. We take advantage of the X-ray induced radiation damage to characterize intermediaries of the catalytic cycle from redox enzymes of the Multicopper Oxidase family.