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Issue 13, 2012
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Design rules for the self-assembly of a protein crystal

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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.

Graphical abstract: Design rules for the self-assembly of a protein crystal

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Publication details

The article was received on 21 Dec 2011, accepted on 13 Feb 2012 and first published on 17 Feb 2012

Article type: Paper
DOI: 10.1039/C2SM07436B
Citation: Soft Matter, 2012,8, 3558-3562

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    Design rules for the self-assembly of a protein crystal

    T. K. Haxton and S. Whitelam, Soft Matter, 2012, 8, 3558
    DOI: 10.1039/C2SM07436B

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