Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Chromatin biomarkers reveal the fingerprints of cancer-associated secretomes isolated by a micropillar-guided platform.

Scientific reports·2026

Same author

Beyond component optimization: systems-level biodesign for lanthanide recovery.

Current opinion in biotechnology·2026

Same author

Visual exoproteomics of <i>Clostridium thermocellum</i> during anaerobic biomass-degradation identifies functional spirosomes.

bioRxiv : the preprint server for biology·2026

Same author

Retinal proteins: Experiment and computation.

Biophysical journal·2026

Same author

The influence of electrical charge on plasmodesma conductivity.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Systematic scale-up and enhanced purification of marine cyanophage P-SSP7.

Frontiers in microbiology·2026

Search research articles

Related Experiment Video

Updated: Apr 26, 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

Femtosecond X-ray diffraction from two-dimensional protein crystals.

Matthias Frank¹, David B Carlson², Mark S Hunter¹

¹Lawrence Livermore National Laboratory , 7000 East Avenue, Livermore, CA 94550, USA.

|July 31, 2014

Summary

Femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) enable new X-ray diffraction data collection from 2-D protein crystals. This "diffract-before-destroy" method bypasses radiation damage for structural analysis without cryo-conditions.

Keywords:

femtosecond crystallography membrane protein single layer X-ray diffraction two-dimensional protein crystal

More Related Videos

$On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature$

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

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

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

Published on: April 24, 2018

Related Experiment Videos

Last Updated: Apr 26, 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

$On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature$

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

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

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

Published on: April 24, 2018

Area of Science:

Structural biology
Biophysics
X-ray crystallography

Background:

Acquiring X-ray diffraction patterns from 2-D protein crystals is challenging due to radiation damage.
Previous methods were limited by sample destruction before sufficient data could be collected.

Purpose of the Study:

To demonstrate a novel method for collecting X-ray diffraction data from 2-D protein crystals.
To overcome radiation damage limitations in X-ray crystallography of 2-D protein arrays.

Main Methods:

Utilized femtosecond X-ray pulses from an X-ray free-electron laser (XFEL).
Employed a "diffract-before-destroy" approach at the Linac Coherent Light Source.
Collected Bragg diffraction data from thin 2-D protein crystal samples at room temperature.

Main Results:

Achieved better than 8.5 Å resolution diffraction patterns from individual 2-D protein crystals.
Successfully collected data from two different 2-D protein crystal samples, each <10 nm thick.
Demonstrated the feasibility of structural analysis without cryogenic conditions.

Conclusions:

Femtosecond XFEL pulses offer a viable method for X-ray diffraction of 2-D protein crystals.
This approach facilitates structural determination of soluble and membrane proteins in 2-D arrays.
Eliminates the need for cryogenic temperatures or 3-D crystal formation for structural studies.