Tominaga, Y. et al. Nat. Photon. 10, 723–726 (2016).

The growth of large, high-quality protein crystals for X-ray diffraction studies is more of an art than a science, requiring extensive testing of different conditions. Tominaga et al. now show how crystal growth can be stimulated with light—more specifically, femtosecond laser ablation. They used femtosecond pulses of laser light to etch one side of a hen egg white lysozyme crystal, which caused disruptions to the crystal lattice. This disruption switched the mechanism of crystal growth from slow two-dimensional nucleation to faster spiral-growth mode. The method produced a hillock-shaped lysozyme crystal that was 30% larger than the original crystal, with quality similar to that of traditionally grown crystals. The approach may find use in traditional structural biology as well as in the materials field.