We report on the first use of carbon-nanotube based films to produce crystals of proteins. The crystals nucleate on the surface of the film. The difficulty of crystallising proteins is a major bottleneck in the determination of the structure and function of biological molecules. The crystallisation of two model proteins and two medically relevant proteins was studied. Quantitative data on the crystallisation times of the model protein lysozyme are also presented. Two types of the nanotube film, one made with the surfactant Triton X-100 (TX-100) and one with gelatin, were tested. Both induce nucleation of the crystal phase at supersaturations at which the protein solution would otherwise remain clear, however the gelatin-based film induced nucleation down to much lower supersaturations for the two model proteins with which it was used. It appears that the interactions of gelatin with the protein molecules are particularly favourable to nucleation. Crystals of the C1 domain of the human cardiac myosin-binding protein-C that diffracted to a resolution of 1.6Å, were obtained on the TX-100 film. This is far superior to the best crystals obtained using standard techniques, which only diffracted to 3.0 Å. Thus, both our nanotube-based films are very promising candidates for future work on crystallising difficult-tocrystallise target proteins.3