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The ability of proteins and other macromolecules to interact with inorganic surfaces is essential to biological function. The proteins involved in these interactions are highly charged and often rich in carboxylic acid side chains^{, , , –}, but the structures of most protein–inorganic interfaces are unknown. We explored the possibility of systematically designing structured protein–mineral interfaces, guided by the example of ice-binding proteins, which present arrays of threonine residues (matched to the ice lattice) that order clathrate waters into an ice-like structure. Here we design proteins displaying arrays of up to 54 carboxylate residues geometrically matched to the potassium ion (K⁺) sublattice on muscovite mica (001). At low K⁺ concentration, individual molecules bind independently to mica in the designed orientations, whereas at high K⁺ concentration, the designs form two-dimensional liquid-crystal phases, which …