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Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
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Updated: Apr 26, 2026

$Microcrystal Electron Diffraction of Small Molecules$

Microcrystal Electron Diffraction of Small Molecules

Published on: March 15, 2021

High-resolution structure determination by continuous-rotation data collection in MicroED.

Brent L Nannenga¹, Dan Shi¹, Andrew G W Leslie²

¹Janelia Research Campus, Howard Hughes Medical Institute, Ashburn VA, USA.

|August 4, 2014

Summary

This summary is machine-generated.

We developed a new continuous rotation method for Microcrystal Electron Diffraction (MicroED) to improve protein structure determination. This enhanced data collection and processing yields more accurate results, advancing structural biology applications.

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$Microcrystal Electron Diffraction of Small Molecules$

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Published on: March 15, 2021

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Published on: March 16, 2022

Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

Microcrystal Electron Diffraction (MicroED) is a powerful technique for determining the three-dimensional structures of proteins using small crystals.
Accurate data collection is crucial for high-resolution structure determination in MicroED.

Purpose of the Study:

To present an improved data collection protocol for MicroED, termed 'continuous rotation'.
To enhance the accuracy and resolution of MicroED data processing.
To facilitate the broader implementation of MicroED in structural biology.

Main Methods:

Developed and implemented a 'continuous rotation' data collection strategy for MicroED.
Utilized the crystallographic software tool MOSFLM for data processing.
Applied the method to the model protein lysozyme for validation.

Main Results:

The continuous rotation method yielded more accurate diffraction data compared to conventional methods.
Improved resolution was achieved for the lysozyme structure model.
Demonstrated the compatibility of the new protocol with existing data processing software.

Conclusions:

The continuous rotation protocol significantly enhances MicroED data quality and structural resolution.
This improved method is poised to accelerate the adoption and application of MicroED in diverse structural biology research.
The findings pave the way for routine high-resolution structure determination of challenging protein targets using MicroED.