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Advances in experimental techniques and in theoretical models have improvedour understanding of protein crystallization. But they have also left openquestions regarding the protein phase behavior and self-assembly kinetics, suchas why (nearly) identical crystallization conditions sometimes result in theformation of different crystal forms. Here, we develop a patchy particle modelwith competing sets of patches that provides a microscopic explanation of thisphenomenon. We identify different regimes in which one or two crystal forms cancoexist with a low-density fluid. Using analytical approximations, we extendour findings to different crystal phases, providing a general framework fortreating protein crystallization when multiple crystal forms compete. Ourresults also suggest different experimental routes for targeting a specificcrystal form, and for reducing the dynamical competition between the two forms,thus facilitating protein crystal assembly.

Competition between monomeric and dimeric crystals in schematic models for globular proteins