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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.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...

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Related Experiment Video

Updated: Feb 28, 2026

Fixed Target Serial Data Collection at Diamond Light Source

Fixed Target Serial Data Collection at Diamond Light Source

Published on: February 26, 2021

High-speed fixed-target serial virus crystallography.

Philip Roedig¹, Helen M Ginn^2,3, Tim Pakendorf¹

¹Photon Science, Deutsches Elektronen-Synchrotron DESY, Hamburg, Germany.

|June 20, 2017

Summary

This summary is machine-generated.

This study introduces a new serial X-ray crystallography method for X-ray free-electron lasers (XFELs). This technique efficiently determines virus crystal structures using minimal sample, enhancing throughput at XFEL facilities.

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Improving High Viscosity Extrusion of Microcrystals for Time-resolved Serial Femtosecond Crystallography at X-ray Lasers

Improving High Viscosity Extrusion of Microcrystals for Time-resolved Serial Femtosecond Crystallography at X-ray Lasers

Published on: February 28, 2019

Related Experiment Videos

Last Updated: Feb 28, 2026

Fixed Target Serial Data Collection at Diamond Light Source

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Published on: February 26, 2021

Author Spotlight: Advancing Protein Structure Analysis for Drug Development

Author Spotlight: Advancing Protein Structure Analysis for Drug Development

Published on: March 8, 2024

Improving High Viscosity Extrusion of Microcrystals for Time-resolved Serial Femtosecond Crystallography at X-ray Lasers

Improving High Viscosity Extrusion of Microcrystals for Time-resolved Serial Femtosecond Crystallography at X-ray Lasers

Published on: February 28, 2019

Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

Serial X-ray crystallography (SFX) is a powerful technique for determining protein and virus structures.
X-ray free-electron lasers (XFELs) offer high-intensity, ultrashort pulses ideal for SFX.
Current limitations in sample delivery and data collection rates can hinder XFEL efficiency.

Purpose of the Study:

To develop and validate a novel serial X-ray crystallography method for X-ray free-electron lasers (XFELs).
To maximize the use of the high repetition rate of XFELs like the Linear Coherent Light Source (LCLS).
To enable structure determination from microgram quantities of sample.

Main Methods:

Utilized a micropatterned silicon chip for sample delivery.
Employed the high-speed Roadrunner goniometer for rapid sample exchange.
Synchronized sample delivery with the XFEL pulse rate (120 Hz).

Main Results:

Successfully determined the crystal structures of bovine enterovirus 2 (BEV2) and cytoplasmic polyhedrosis virus type 18 polyhedrin.
Achieved total data collection times of under 14 minutes for BEV2 and 10 minutes for polyhedrin.
Demonstrated the method's effectiveness with microgram sample quantities.

Conclusions:

The developed method significantly enhances sample throughput at XFEL facilities.
This approach broadens the applicability of serial femtosecond crystallography to challenging projects with limited sample.
Efficient synchronization of sample delivery with XFEL repetition rates is crucial for maximizing beamtime utilization.