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

$X-ray Diffraction of Biological Samples$ 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 crystal...

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...

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...

You might also read

Related Articles

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

Sort by

Same author

Decoding Enzyme-Inhibitor Kinetic Mechanisms by Isothermal Titration Calorimetry: The Case of SARS-CoV-2 3CL<sup>pro</sup>.

Analytical chemistry·2026

Same author

Assessing Metal Ion Assignment Accuracy in Protein Data Bank Models via Elemental Spectroscopy.

Journal of chemical information and modeling·2026

Same author

Allosteric Protein Chemical Shift Perturbations are Ubiquitous.

bioRxiv : the preprint server for biology·2026

Same author

The NMR Exchange Format (NEF): Specification and Applications.

bioRxiv : the preprint server for biology·2026

Same author

Hidden structural states of proteins revealed by conformer selection.

Nature communications·2026

Same author

Loop Plasticity Drives Paralog-Specific Recognition in BET ET Domains.

Journal of chemical information and modeling·2026

Same journal

Untreated Rosehip Powder/Poly(Lactic Acid)/Poly(3-Hydroxybutyrate-Co-4-Hydroxybutyrate) Electrospun Mats for Wound Dressing Applications.

Biopolymers·2026

Same journal

Synthesis, Characterization, and Antidiabetic Evaluation of Sequence-Modified Liraglutide Analogs in a Drosophila melanogaster Model.

Biopolymers·2026

Same journal

Fabrication of an Antibacterial Alginate/Chitosan Hydrogel Dressing Loaded With CuO Nanoparticles for Wound Dressing Applications.

Biopolymers·2026

Same journal

Effect of Chitosan-Alginate Polyelectrolyte Complex Formation and Multilayer Polymer Configuration on the Characteristics of 3D-Printed Metronidazole-Loaded Periodontal Films.

Biopolymers·2026

Same journal

Phenolic Grafting of Oxidized Cellulose Nanofibers Using Ferulic Acid: Structural and Antioxidant Analysis Toward Bioactive Nanomaterials.

Biopolymers·2026

Same journal

Detection of a Target Nucleic Acid by Ligation-Assisted Fluorescence Enhancement of a Peptide Nucleic Acid (PNA) Twin Probe via Disulfide Binding.

Biopolymers·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 3, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Small angle X-ray scattering as a complementary tool for high-throughput structural studies.

Thomas D Grant¹, Joseph R Luft, Jennifer R Wolfley

¹Hauptman-Woodward Medical Research Institute, 700 Ellicott St., Buffalo, NY 14203, USA.

|April 5, 2011

Summary

This summary is machine-generated.

Small angle X-ray scattering (SAXS) complements high-resolution protein structures. This high-throughput technique provides valuable molecular size and conformation data, enhancing functional interpretation when structural information is limited.

More Related Videos

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Related Experiment Videos

Last Updated: Jun 3, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Area of Science:

Biochemistry and structural biology
Macromolecular structure determination

Background:

Structural crystallography and NMR spectroscopy are primary methods for molecular structure determination.
These techniques have limitations, leaving many proteins structurally uncharacterized.
Small angle X-ray scattering (SAXS) offers a solution-based approach for studying proteins in solution.

Purpose of the Study:

To evaluate the accuracy of SAXS-derived molecular envelopes using existing crystallographic and NMR data.
To highlight the complementary structural information provided by SAXS.
To assess SAXS's utility in high-throughput structural characterization.

Main Methods:

Application of small angle X-ray scattering (SAXS) in a high-throughput manner.
Analysis of 28 proteins with available structural data from crystallography and/or NMR.
Reconstruction of low-resolution molecular envelopes from SAXS data.

Main Results:

SAXS molecular envelopes showed good agreement with high-resolution crystallographic and NMR structures.
SAXS provided complementary data on protein size and conformational flexibility.
The study demonstrated the feasibility of using SAXS for high-throughput structural analysis.

Conclusions:

SAXS is a valuable low-resolution technique for structural biology.
It effectively complements high-resolution methods by providing insights into protein size and conformation.
SAXS enhances the functional interpretation of protein structures, especially for uncharacterized samples.