The review presents the important unique results of the cycle of research led by M.V. Kovalchuk on the fundamental patterns of protein interactions and the protein self-assembly during the formation of ordered systems. A radically new scientific and methodological approach to multiscale studies of the mechanisms of organization and the structures of protein systems was developed and tested. This approach is based on the analysis of their crystal structures and the application of a combination of X-ray, synchrotron, and neutron techniques and molecular modeling methods and deals with the formation of a pre-crystallization phase, i.e., the formation of precursor clusters, 3D fragments of the future structure of the material, in the initial step of the atomic-molecular organization of the system to form an ordered crystal structure. The structure of the pre-crystallization phase, the mechanisms of the formation of its components, and the thermodynamic parameters of this system during the crystal and film formation were studied in relation to the model protein lysozyme. The developed approach was efficiently applied to the description of precursor clusters in the pre-crystallization phase of a series of other proteins, and then the proposed structure was experimentally determined and confirmed.
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