The described system provides a rare example of protein-directed ordered assembly of fullerenes. The new-engineered CTPR proteins with tyrosine clamps allows to steer the assembly of fullerenes into crystalline arrangements, while promoting innate fullerene interactions. As a result, the hybrid material supports strong photocurrents, allowing photo-generated charge carriers to move through fullerene contacts. Thus, the presented system brings protein research one step closer to supramolecular assemblies governed by rationally designed proteins. In addition, to the best of our knowledge the CTPR-fullerene hybrid assemblies present a first instance of crystalline assemblies observed in liquid phase. Despite the advances in successful protein design, it is noteworthy that correct choice of a starting structure plays a crucial role. Based on the current and multiple other supramolecular assemblies, using repeat proteins as a scaffold for supramolecular ordering seems to be the winning strategy. Protein design and production Molecular model of tyrosine mutations was build using Pymol. E2Y, N6A and N9Y point mutations constituting the mutated residues were introduced into C1 consensus repeat through QuikChange site-directed mutagenesis. CTPR8 proteins were constructed by sequential ligation of consensus and mutated C1 sequences into pPro-EX-HTa vector.