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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

824
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
824
X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

3.8K
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...
3.8K

You might also read

Related Articles

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

Sort by
Same author

A user-friendly goniometer-compatible fixed-target platform for macromolecular crystallography at synchrotrons.

Journal of applied crystallography·2026
Same author

Erratum: A simple goniometer-compatible flow cell for serial synchrotron X-ray crystallography. Corrigendum.

Journal of applied crystallography·2025
Same author

Preface to special topic: Celebrating the work and achievements of Keith Moffat.

Structural dynamics (Melville, N.Y.)·2025
Same author

Unveiling long-range forces in light-harvesting proteins: Pivotal roles of temperature and light.

Science advances·2025
Same author

Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.

Nature communications·2025
Same author

Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate.

Nature communications·2024

Related Experiment Video

Updated: Jun 19, 2025

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

17.9K

Appraising protein conformational changes by resampling time-resolved serial x-ray crystallography data.

Adams Vallejos1, Gergely Katona1, Richard Neutze1

  • 1Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, 40530 Gothenburg, Sweden.

Structural Dynamics (Melville, N.Y.)
|July 26, 2024
PubMed
Summary
This summary is machine-generated.

Time-resolved serial femtosecond crystallography reveals how protein conformational changes relate to activation. New methods improve accuracy in analyzing these dynamic structural shifts.

More Related Videos

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.0K
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

9.9K

Related Experiment Videos

Last Updated: Jun 19, 2025

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

17.9K
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

4.0K
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

9.9K

Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • Time-resolved X-ray crystallography is advancing the study of macromolecular conformational changes.
  • Serial crystallography at X-ray free electron lasers and synchrotrons enables new insights.
  • Successful studies require microcrystal growth, synchronized excitation, and robust interpretation tools.

Purpose of the Study:

  • To compare structural refinement methods using time-resolved serial femtosecond crystallography data.
  • To analyze conformational changes in bacteriorhodopsin microcrystals.
  • To develop and validate tools for interpreting time-resolved crystallographic data.

Main Methods:

  • Utilized time-resolved serial femtosecond crystallography on bacteriorhodopsin microcrystals.
  • Compared partial occupancy refinement with refinement against extrapolated data.
  • Employed resampling strategies for coordinate uncertainty estimation.
  • Applied singular value decomposition to difference Fourier electron density maps.
  • Analyzed difference Fourier and Polder omit maps for transient water molecules.

Main Results:

  • Demonstrated an inverse relationship between conformational change amplitude and activated state occupancy.
  • Showed agreement between partial occupancy and extrapolated data refinement within coordinate errors.
  • Illustrated how singular value decomposition minimizes phase bias in electron density maps.
  • Quantified residual densities for transient water molecules using advanced map analysis.

Conclusions:

  • Developed and validated tools for interpreting time-resolved crystallographic data.
  • Provided insights into the dynamics of protein conformational changes.
  • Aimed to assist researchers in confidently interpreting electron density differences as functional changes.