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Related Experiment Video

Updated: May 5, 2026

A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline

A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline

Published on: June 17, 2021

Gently does it for submicron crystals.

Oliver B Zeldin¹, Axel T Brunger

¹Oliver B Zeldin is in the Department of Molecular and Cellular Physiology and the Howard Hughes Medical Institute, Stanford University, Stanford, United States zeldin@stanford.edu.

|November 21, 2013

Summary

This summary is machine-generated.

This study refined protein structure using electron diffraction from tiny crystals. A weak electron beam enabled collecting numerous patterns for accurate structural determination.

Keywords:

electron cryomicroscopy (cryo EM)electron crystallography electron diffraction method development protein structure

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Last Updated: May 5, 2026

A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline

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Published on: June 17, 2021

$Microcrystallography of Protein Crystals and In Cellulo Diffraction$

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Published on: July 21, 2017

$Microcrystal Electron Diffraction of Small Molecules$

Microcrystal Electron Diffraction of Small Molecules

Published on: March 15, 2021

Area of Science:

Structural biology
Crystallography
Electron diffraction

Background:

Determining protein structures is crucial for understanding biological functions.
Traditional methods often require large, high-quality crystals, which are difficult to obtain.
Electron diffraction offers a potential alternative for structure determination.

Purpose of the Study:

To refine a protein structure using electron diffraction data.
To demonstrate the feasibility of using a weak electron beam for data collection.
To overcome limitations associated with crystal size in structural biology.

Main Methods:

Collected electron diffraction data from sub-micron-sized 3D crystals.
Utilized a very weak electron beam to minimize sample damage.
Processed a large number of diffraction patterns for structure refinement.

Main Results:

Successfully refined a protein structure.
Demonstrated the utility of weak-beam electron diffraction for structural analysis.
Showcased the ability to obtain structural information from small crystal samples.

Conclusions:

Weak-beam electron diffraction is a viable method for protein structure determination.
This technique expands the possibilities for studying proteins that form small crystals.
Advances in electron diffraction open new avenues in structural biology research.