Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

X-ray Diffraction of Biological Samples01:10

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...
Protein Folding01:22

Protein Folding

Overview
X-ray Crystallography02:18

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...

You might also read

Related Articles

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

Sort by
Same author

Studies of the structural properties and stability of the molybdenum transport protein ModA from Oleidesulfovibrio alaskensis G20 upon metal binding.

Archives of biochemistry and biophysics·2025
Same author

Compact polyethylenimine-complexed mRNA vaccines.

Nature nanotechnology·2025
Same author

A genetically encoded anomalous SAXS ruler to probe the dimensions of intrinsically disordered proteins.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

Small-angle x-ray scattering investigation of the integration of free fatty acids in polysorbate 20 micelles.

Biophysical journal·2024
Same author

Small conformational changes in IgG1 detected as acidic charge variants by cation exchange chromatography.

Analytical biochemistry·2023
Same author

Probing the conformational changes of <i>in vivo</i> overexpressed cell cycle regulator 6S ncRNA.

Frontiers in molecular biosciences·2023

Related Experiment Video

Updated: Jul 15, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

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

Published on: November 5, 2018

Structural characterization of flexible proteins using small-angle X-ray scattering.

Pau Bernadó1, Efstratios Mylonas, Maxim V Petoukhov

  • 1European Molecular Biology Laboratory, Hamburg Outstation, 22603 Hamburg, Germany. pbernado@pcb.ub.es

Journal of the American Chemical Society
|April 7, 2007
PubMed
Summary

The ensemble optimization method (EOM) quantitatively characterizes flexible proteins in solution using small-angle X-ray scattering (SAXS). This approach models protein flexibility by analyzing multiple conformations, providing detailed structural insights.

More Related Videos

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

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 and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution
12:53

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution

Published on: January 8, 2013

Related Experiment Videos

Last Updated: Jul 15, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

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

Published on: November 5, 2018

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

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 and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution
12:53

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution

Published on: January 8, 2013

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • High-resolution structural techniques are limited for flexible macromolecular systems like intrinsically disordered or multidomain proteins.
  • Characterizing the conformational heterogeneity of such proteins in solution remains a significant challenge.

Purpose of the Study:

  • To introduce and validate the ensemble optimization method (EOM) for quantitative structural analysis of flexible proteins.
  • To utilize small-angle X-ray scattering (SAXS) data to characterize protein flexibility and conformational ensembles.

Main Methods:

  • Developed the ensemble optimization method (EOM), employing a genetic algorithm to select protein conformations from a large configurational pool.
  • Utilized small-angle X-ray scattering (SAXS) to capture the scattering pattern influenced by protein flexibility.
  • Incorporated quantitative criteria for analyzing EOM-selected models and determining the optimal number of conformers.
  • Integrated data from deletion mutants to gain local structural information.

Main Results:

  • EOM successfully characterizes protein flexibility in solution by modeling the coexistence of multiple conformations.
  • The method effectively analyzes unfolded and multidomain proteins, distinguishing between rigid and flexible structures.
  • Demonstrated the ability to assess interdomain contacts in multidomain proteins.

Conclusions:

  • EOM provides a robust framework for quantitatively analyzing the structural ensemble of flexible proteins using SAXS.
  • The method offers valuable insights into protein conformational dynamics and interactions, overcoming limitations of high-resolution techniques.