Crystallization of cyclosporin A in lyotropic reverse hexagonal liquid crystals

In this communication we demonstrate for the first time that lyotropic reverse hexagonal mesophase can serve as a crystallization medium for a hydrophobic peptide, resulting in high quality single crystals suitable for crystallographic analysis. The obtained crystals of cyclosporin A enabled excellent X-ray data collection, diffracting to a resolution limit of 1.0 . Current findings open a new perspective in the field of crystallization of biological macromolecules in lyotropic mesophases.