Crystallography may be the gold standard of protein structure determination, but obtaining the necessary high-quality crystals is akin to prospecting for the precious mineral. The fields of structural biology and soft matter have independently sought out fundamental principles to rationalize the process, but the conceptual differences and the limited crosstalk between the two disciplines have  prevented a comprehensive understanding of the phenomenon to emerge. Here we conduct a computational study of proteins from the rubredoxin family that bridges the two fields. Using atomistic simulations, we characterize the crystal contacts, and then parameterize patchy particle models. Comparing the phase diagrams of these  models with experimental results enables us to critically examine the assumptions behind the two approaches and to reveal key features of protein-protein interactions that facilitate their crystallization .
 The fields of structural biology and soft matter have independently sought out fundamental principles to rationalize protein crystallization. Yet the conceptual differences and the limited overlap between the two disciplines have thus far prevented a comprehensive understanding of the phenomenon to emerge. We conduct a computational study of proteins from the rubredoxin family that bridges the two fields. Using atomistic simulations, we characterize their crystal contacts, and accordingly parameterize patchy particle models. Comparing the phase diagrams of these schematic models with experimental results enables us to critically examine the assumptions behind the two approaches . The study also reveals features of protein-protein interactions that can be leveraged to crystallize proteins more generally .
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