Crystallization achieves precise, long-range ordering of molecules via self-assembly and can potentially be leveraged to engineer materials with controlled molecular orientation and symmetry. Biopolymer crystals in particular can provide a precise framework for controlling molecular orientation. Here we present a computational strategy for designing predetermined protein crystal structures by explicitly engineering the crystal contacts. A protein is designed de novo to form a crystal possessing a polar, layered P6 space group. For an ensemble of protein orientations consistent with this targeted crystalline structure, the sequence-structure energy landscape is characterized by computational protein design. Candidate proteins are identified from minima on this landscape. The experimental characterization is presented, and the crystallographic structure of one designed protein is compared with the computational model structure to reveal sub-nanometer precision. This �landscape� approach can guide the design of proteins that self-assemble into targeted crystalline lattices and facilitate advances towards engineering highly ordered biomaterials.

Engineering crystalline biomaterials via computational protein design

244th National Meeting (2012)

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