Fabrication of crystalline materials with distinct dimensionalities and tailorable structural, physical and chemical properties represents a major goal in fundamental and applied sciences. We report here the bottom-up self-assembly of unsupported, two-dimensional protein lattices with precise spatial arrangements and patterns through a readily accessible design strategy. Three single- or double-point mutants of the soluble, C4 symmetric protein RhuA were designed to assemble via different modes of intermolecular interactions (single disulfide (C98RhuA), double disulfide (F88/C98RhuA) and metal coordination (H63/H98RhuA) ) into crystalline, two-dimensional arrays in a chemically tunable fashion. Owing to the flexibility of the single disulfide interactions, the lattices of one of the variants (C98RhuA) are essentially defect-free and undergo substantial but highly correlated changes in molecular arrangement and porosity, yielding a Poisson’s ratio of –1, the lowest thermodynamically possible value for an isotropic material.

Design and construction of coherently dynamic, auxetic two-dimensional protein crystals

251st National Meeting (2016)

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