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Related Experiment Video

Updated: Feb 4, 2026

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments

Published on: February 4, 2021

Megahertz serial crystallography.

Max O Wiedorn^1,2,3, Dominik Oberthür¹, Richard Bean⁴

¹Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Notkestrasse 85, 22607, Hamburg, Germany.

Nature Communications

|October 4, 2018

Summary

This summary is machine-generated.

High-quality protein structures can now be determined using megahertz X-ray pulses from the European X-ray Free-Electron Laser. This breakthrough enables megahertz serial femtosecond crystallography (SFX) for advanced molecular studies.

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Last Updated: Feb 4, 2026

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments

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Published on: February 4, 2021

Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography

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Published on: September 20, 2016

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Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

Published on: March 20, 2021

Area of Science:

Structural Biology
X-ray Science
Biochemistry

Background:

The European X-ray Free-Electron Laser (XFEL) offers unprecedented megahertz X-ray pulse repetition rates.
Previous feasibility of high-quality diffraction data collection at these rates was uncertain.

Purpose of the Study:

To demonstrate the feasibility of obtaining high-quality diffraction data at megahertz pulse repetition rates.
To validate megahertz serial femtosecond crystallography (SFX) for structure determination.

Main Methods:

Utilized the European XFEL operating conditions.
Collected diffraction data from lysozyme and a beta-lactamase complex.
Performed structure determination using megahertz SFX.

Main Results:

Successfully obtained high-quality diffraction data at megahertz pulse rates.
Determined the structures of lysozyme and a novel beta-lactamase complex.
Demonstrated the viability of megahertz SFX for structure determination.

Conclusions:

Megahertz SFX is a viable technique for reliable structure determination.
This advancement facilitates substrate screening and molecular dynamics studies.
Opens new avenues for research using high-repetition-rate X-ray sources.