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Updated: Jun 22, 2025

Microcrystallography of Protein Crystals and In Cellulo Diffraction
Published on: July 21, 2017
3D Nanocrystallography and the Imperfect Molecular Lattice
Niko Vlahakis1, James Holton2,3,4, Nicholas K Sauter2
1Department of Chemistry and Biochemistry; UCLA-DOE Institute for Genomics and Proteomics; and STROBE, NSF Science and Technology Center, University of California, Los Angeles, California, USA;
None:
Crystallographic analysis relies on the scattering of quanta from arrays of atoms that populate a repeating lattice. While large crystals built of lattices that appear ideal are sought after by crystallographers, imperfections are the norm for molecular crystals. Additionally, advanced X-ray and electron diffraction techniques, used for crystallography, have opened the possibility of interrogating micro- and nanoscale crystals, with edges only millions or even thousands of molecules long. These crystals exist in a size regime that approximates the lower bounds for traditional models of crystal nonuniformity and imperfection. Accordingly, data generated by diffraction from both X-rays and electrons show increased complexity and are more challenging to conventionally model. New approaches in serial crystallography and spatially resolved electron diffraction mapping are changing this paradigm by better accounting for variability within and between crystals. The intersection of these methods presents an opportunity for a more comprehensive understanding of the structure and properties of nanocrystalline materials.
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