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Determination of Crystal Structures

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...

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...

$X-ray Diffraction of Biological Samples$ 01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are scattered by the electron clouds around the sample atoms. The X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal...

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Related Experiment Video

Updated: Mar 1, 2026

$Measurements of Long-range Electronic Correlations During Femtosecond Diffraction Experiments Performed on Nanocrystals of Buckminsterfullerene$

Measurements of Long-range Electronic Correlations During Femtosecond Diffraction Experiments Performed on Nanocrystals of Buckminsterfullerene

Published on: August 22, 2017

Structure Determination Using X-Ray Free-Electron Laser Pulses.

Henry N Chapman^1,2,3

¹Center for Free-Electron Laser Science, DESY, Hamburg, 22607, Germany. henry.chapman@desy.de.

Methods in Molecular Biology (Clifton, N.J.)

|June 3, 2017

Summary

This summary is machine-generated.

Intense X-ray free-electron laser pulses enable high-dose macromolecular crystallography without cooling. Serial crystallography captures diffraction data from many crystals, enabling time-resolved studies and new phasing opportunities.

Keywords:

Coherent diffractive imaging Microcrystallography Phasing Radiation damage Serial crystallography XFEL

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$Synchrotron X-ray Microdiffraction and Fluorescence Imaging of Mineral and Rock Samples$

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$Measurements of Long-range Electronic Correlations During Femtosecond Diffraction Experiments Performed on Nanocrystals of Buckminsterfullerene$

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$Synchrotron X-ray Microdiffraction and Fluorescence Imaging of Mineral and Rock Samples$

Synchrotron X-ray Microdiffraction and Fluorescence Imaging of Mineral and Rock Samples

Published on: June 19, 2018

Area of Science:

Structural biology
X-ray crystallography
Biophysics

Background:

Conventional X-ray crystallography is limited by radiation damage to samples.
Macromolecular crystals often require cryogenic cooling to mitigate damage.
Free-electron lasers (FELs) produce intense, ultrashort X-ray pulses.

Purpose of the Study:

To explore the advantages of using intense X-ray pulses for macromolecular crystallography.
To investigate the serial crystallography approach for collecting diffraction data.
To assess the potential for time-resolved studies and novel phasing methods.

Main Methods:

Utilizing femtosecond X-ray pulses from FELs to outrun radiation damage.
Employing serial crystallography to collect diffraction patterns from numerous individual crystals.
Developing methods for rapid sample replenishment and low-background data acquisition.

Main Results:

High doses are tolerable, allowing the use of smaller crystals and eliminating the need for cooling.
Serial crystallography effectively consolidates millions of weak diffraction patterns.
The method supports time-resolved measurements from picoseconds to seconds.

Conclusions:

Intense X-ray pulses and serial crystallography overcome limitations of conventional methods.
This approach significantly advances macromolecular structure determination and time-resolved studies.
Future developments promise expanded capabilities for structural biology research.