Playing Tetris with protein nanocrystals

New research by scientists from the VIB-VUB Center for Structural Biology (Belgium), the Radboud University (Netherlands), Institut de Biologie Structurale and The Institut des sciences de la Terre de Grenoble, ISTerre/OSUG (CNRS/IRD/Université Grenoble Alpes/Université Savoie Mont Blanc) (Grenoble) using cryo-electron microscopy now demonstrates that these protein crystal nuclei don’t have to work in isolation: the presence of nearby nuclei can help early-stage protein crystals find their ’shape’.

Protein crystallization is a remarkable feat of nature. For proteins crystals to form, each individual protein has to find others and they have to assemble into a stable pattern, a lattice. Finding this pattern is called the nucleation stage.

When these small crystals approach each other, they orient themselves relative to the orientation of their neighbors’ lattices. Similar to the building blocks in a game of 3D Tetris trying to form a macroscopic crystal. But, as every iteration of oriented attachment generates more and more complex geometries, a point is reached where these nanocrystals can no longer dock perfectly with each other, ushering in the formation of a protein mesocrystal driven by imperfect oriented attachment that would probably result in the mosaicity commonly found in protein crystals.

Reference

Nucleation of protein mesocrystals via oriented attachment. Van Driessche et al. 2. Nature Communications, 2021. DOI : 10.1038/s41467-021-24171-z

This was originally published by INSU.