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Changes in lattice structure across sub-regions of protein crystals arechallenging to assess when relying on whole crystal measurements. Because ofthis difficulty, macromolecular structure determination from protein micro andnano crystals requires assumptions of bulk crystallinity and domain blocksubstructure. To evaluate the fidelity of these assumptions in proteinnanocrystals we map lattice structure across micron size areas of cryogenicallypreserved three-dimensional peptide crystals using a nano-focused electronbeam. This approach produces diffraction from as few as 1,500 molecules in acrystal, is sensitive to crystal thickness and three-dimensional latticeorientation. Real-space maps reconstructed from unsupervised classification ofdiffraction patterns across a crystal reveal regions of crystal order/disorderand three-dimensional lattice reorientation on a 20nm scale. The latticenano-ripples observed in micron-sized macromolecular crystals provide a directview of their plasticity. Knowledge of these features is a first step tounderstanding crystalline macromolecular self-assembly and improving thedetermination of structures from protein nano and microcrystals from single orserial crystal diffraction.

Lattice nano-ripples revealed in peptide microcrystals by scanning electron nanodiffraction