Room temperature protein electron crystallography

Compared to X-ray crystallography, electron crystallography can be performed on nanometer-sized crystals and can provide additional information, such as ion valency, from the resulting Coulomb potential map (Acta Cryst. D 2021, 77, 75- 85). Although electron crystallography has successfully resolved three-dimensional protein structures from vitrified crystals, its widespread use as a structural biology tool is limited. One of the reasons for this is the fragility of these crystals, which can be easily damaged by mechanical stress, temperature changes, etc. In this publication, in collaboration with Nanomegas in Belgium, John Hopkins University in the United States and Universitat Rovira in Spain, researchers from the MEM group and the GSY group at IBS used graphene to encapsulate lysozyme nanocrystals in their mother liquor as an alternative to vitrification and cryo-electron microscopy (Nat Commun. 2023 ; 14, 5641). They then carried out electron diffraction experiments on these nanocrystals at room temperature. Using the hybrid pixel detector installed on the F20 microscope at the IBS/ISBG electron microscopy platform, these experiments yielded diffraction patterns with a resolution of up to 3Å, with indexing possible using a pattern matching algorithm.

High-Resolution Electron Diffraction of Hydrated Protein Crystals at Room Temperature. Plana-Ruiz S, Gómez-Pérez A, Budayova-Spano M, Foley DL, Portillo-Serra J, Rauch E, Grivas E, Housset D, Das PP, Taheri ML, Nicolopoulos S, Ling WL. ACS Nano 2023 ;17(24):24802-24813.

Contact : Wai Li Ling (IBS/Methods and Electron Microscopy Group)