Protein-directed self-assembly of a fullerene crystal

Kook Han Kim, Dong Kyun Ko, Yong Tae Kim, Nam Hyeong Kim, Jaydeep Paul, Shao Qing Zhang, Christopher B. Murray, Rudresh Acharya, William F. Degrado, Yong Ho Kim, Gevorg Grigoryan

Research output: Contribution to journalArticlepeer-review

56 Scopus citations


Learning to engineer self-assembly would enable the precise organization of molecules by design to create matter with tailored properties. Here we demonstrate that proteins can direct the self-assembly of buckminsterfullerene (C 60) into ordered superstructures. A previously engineered tetrameric helical bundle binds C 60 in solution, rendering it water soluble. Two tetramers associate with one C 60, promoting further organization revealed in a 1.67-Å crystal structure. Fullerene groups occupy periodic lattice sites, sandwiched between two Tyr residues from adjacent tetramers. Strikingly, the assembly exhibits high charge conductance, whereas both the protein-alone crystal and amorphous C 60 are electrically insulating. The affinity of C 60 for its crystal-binding site is estimated to be in the nanomolar range, with lattices of known protein crystals geometrically compatible with incorporating the motif. Taken together, these findings suggest a new means of organizing fullerene molecules into a rich variety of lattices to generate new properties by design.

Original languageEnglish (US)
Article number11429
JournalNature communications
StatePublished - Apr 26 2016

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • General Biochemistry, Genetics and Molecular Biology
  • General Physics and Astronomy


Dive into the research topics of 'Protein-directed self-assembly of a fullerene crystal'. Together they form a unique fingerprint.

Cite this