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X-ray Crystallography

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
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$X-ray Diffraction of Biological Samples$ 01:10

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Related Experiment Video

Updated: Dec 10, 2025

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

A Workflow for Protein Structure Determination From Thin Crystal Lamella by Micro-Electron Diffraction.

Emma V Beale¹, David G Waterman^2,3, Corey Hecksel⁴

¹Diamond Light Source, Harwell Science and Innovation Campus, Didcot, United Kingdom.

Frontiers in Molecular Biosciences

|August 28, 2020

Summary

Microcrystal electron diffraction (MicroED) now allows atomic-resolution analysis of any protein crystal size or shape. This new workflow overcomes previous limitations, enabling routine structure determination for biological samples.

Keywords:

cryoEM cryoFIB crystallography lamella microED nanocrystals proteinase K

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Last Updated: Dec 10, 2025

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

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Published on: July 21, 2017

$Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography$

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$Microcrystal Electron Diffraction of Small Molecules$

Microcrystal Electron Diffraction of Small Molecules

Published on: March 15, 2021

Area of Science:

Structural biology
Biophysics
Materials science

Background:

Microcrystal electron diffraction (MicroED) is a powerful technique for atomic-resolution structural analysis.
Previous MicroED applications were limited to thin protein nanocrystals (needles or plates).
Existing data processing software is not optimized for unique electron diffraction data effects.

Purpose of the Study:

To present an integrated workflow for MicroED enabling routine atomic structure determination of protein crystals.
To overcome limitations of crystal size and shape in MicroED analysis.
To demonstrate the advantage of using protein crystal lamellae over nanocrystals.

Main Methods:

Cryo-focused ion beam milling for sample preparation.
Data collection using a standard Ceta-D detector.
Data processing with the DIALS software suite.

Main Results:

Developed and demonstrated an integrated MicroED workflow.
Successfully determined the structure of proteinase K to 2.0 Å resolution.
Showcased the utility of protein crystal lamellae for MicroED analysis.

Conclusions:

The presented workflow enables routine atomic structure determination of protein crystals of any size and shape using MicroED.
This integrated approach expands the applicability of MicroED in structural biology.
Protein crystal lamellae are advantageous over nanocrystals for MicroED analysis.