Electron Crystallography for Structure Determination - From Inorganics to Proteins

X-ray crystallography is a powerful method for solving inorganic, micro-molecular and macromolecular structures from 3D crystals. However, a historical challenge is to obtain crystals of suitable size and suitable solidity (in the protein case) to allow X-ray data collection. More specifically, the growth optimization of protein crystals from microcrystals is often intricate/troublesome and not always successful. In the past decades, Zou and Hovmöller’s group has developed electron crystallographic methods for structure determination of inorganic micron- and nano-sized crystals. In 2010, the Rotation Electron Diffractions (RED) technique was developed, which combines mechanical goniometer tilt with fine electron beam tilt (0.01 – 0.20°) to sample 3D reciprocal lattice of micron- and nano-sized single crystals. Zou’s group has applied the RED data for ab initio solution of more than 80 complex inorganic structures. In 2015, we implemented the continuous RED (cRED) technique based on RED and literatures by Nannenga et al.(2014) and Gemmi et al.(2015), which extended our ability to determine structures of small organic molecules and proteins from micron- and nano-sized 3D crystals. Hongyi Xu(1), Hugo Lebrette(2), Taimin Yang(1), JingJing Zhao(1), Viktor Bengtsson(1), Wei Wan(1), Stef Smeets(1), Vivek Srinivas(2), Sven Hovmöller(1), Martin Högbom(2), Xiaodong Zou(1) 1. Department of Materials and Environmental Chemistry, Stockholm University 2. Department of Biochemistry and Biophysics, Stockholm University