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- W2112121442 startingPage "3558" @default.
- W2112121442 abstract "Theories of protein crystallization based on spheres that form close-packed crystals predict optimal assembly within a `slot' of second virial coefficients and enhanced assembly near the metastable liquid-vapor critical point. However, most protein crystals are open structures stabilized by anisotropic interactions. Here, we use theory and simulation to show that assembly of one such structure is not predicted by the second virial coefficient or enhanced by the critical point. Instead, good assembly requires that the thermodynamic driving force be on the order of the thermal energy and that interactions be made as nonspecific as possible without promoting liquid-vapor phase separation." @default.
- W2112121442 created "2016-06-24" @default.
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- W2112121442 date "2012-01-01" @default.
- W2112121442 modified "2023-10-14" @default.
- W2112121442 title "Design rules for the self-assembly of a protein crystal" @default.
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- W2112121442 doi "https://doi.org/10.1039/c2sm07436b" @default.
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