In collaboration with David Baker (HHMI, UW) we are designing genetically encoded self assembling proteins for cellular microcircuitry. 
We describe a general computational method for designing proteins that self-assemble to a desired symmetric architecture. Protein building blocks are docked together symmetrically to identify complementary packing arrangements, and low-energy protein-protein interfaces are then designed between the building blocks in order to drive self-assembly. Here we use trimeric protein building blocks to design a 24-subunit, 13 nm diameter complex with octahedral symmetry and two related variants of a 12-subunit, 11 nm diameter complex with tetrahedral symmetry. The designed proteins assembled to the desired oligomeric states in solution, and crystal structures of the complexes revealed that the resulting materials closely match the design models. The method can be used to design a wide variety of self-assembling protein nanomaterials. (Figure 10)
Relevant papers
1. King NP., Sheffler W., Sawaya MR., Vollmar BS., Sumida JP., Andre I., Gonen T., Yeates TO. And Baker D. (2012) Computational design of self-assembling protein nanomaterials with atomic level accuracy. Science. 336: 1171 – 1174.
2. King NP, Bale J, Sheffler W, McNamara DE., Gonen S., Gonen T., Yeates TO. and Baker D. Accurate design of coassembling multi-component protein nanomaterials. Nature 510 (7503): 103 – 108.
3. Bale JB., Park RU., Liu Y., Gonen S., Gonen T., Cascio D., King NP., Yeates TO., and Baker D (2015) Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression. Protein Science – In Press.
4. Gonen S., DiMIao F., Gonen T* and Baker D*. Design of ordered two-dimensional arrays mediated by noncovalent protein-protein interfaces. Science 348 (6241): 1365 - 1368 (2015)