A complete micro-electron diffraction (MicroED) solution for fast structure determination of macromolecules and small molecules

Abstract

X - ray diffraction using synchrotron radiation established a routine single-crystal structure determination workflow for small and macromolecules; however, these experiments require large, well -ordered crystals (50 - 100 μm). Growing large protein crystals is a critical bottleneck that is either time-consuming or challenging to overcome, and often smaller crystals are more attainable. Although microfocus beamlines can analyze crystals as small as 10 - 50 μm, they are prone to radiation damage or diffract X - rays weakly, limiting achievable resolution. Electrons are more advantageous than X - rays for the analysis of very small crystals (well below 1 μm in size) because accelerated electrons scatter more readily than X - rays, resulting in a stronger signal from thinner samples. Micro - or nano-crystal elect ron diffraction (MicroED) is thus well - suited for the analysis of small crystals, producing high-resolution 3D structures of small chemical compounds or biological macromolecules. MicroED