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

The Quantum-Mechanical Model of an Atom02:45

The Quantum-Mechanical Model of an Atom

42.0K
Shortly after de Broglie published his ideas that the electron in a hydrogen atom could be better thought of as being a circular standing wave instead of a particle moving in quantized circular orbits, Erwin Schrödinger extended de Broglie’s work by deriving what is now known as the Schrödinger equation. When Schrödinger applied his equation to hydrogen-like atoms, he was able to reproduce Bohr’s expression for the energy and, thus, the Rydberg formula governing hydrogen spectra.
42.0K
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
The de Broglie Wavelength02:32

The de Broglie Wavelength

25.3K
In the macroscopic world, objects that are large enough to be seen by the naked eye follow the rules of classical physics. A billiard ball moving on a table will behave like a particle; it will continue traveling in a straight line unless it collides with another ball, or it is acted on by some other force, such as friction. The ball has a well-defined position and velocity or well-defined momentum, p = mv, which is defined by mass m and velocity v at any given moment. This is the typical...
25.3K

You might also read

Related Articles

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

Sort by
Same author

A minimal chemo-mechanical Markov model for rotary catalysis of F<sub>1</sub>-ATPase.

Nature communications·2026
Same author

Hierarchical multi-timescale structural dynamics of the disordered N-terminal of p53.

Nature communications·2026
Same author

Improving Conformational Ensembles of Folded Proteins in Go̅Martini.

Journal of chemical theory and computation·2026
Same author

Braess' Paradox in Enzyme Kinetics: Asymmetry from Population Balance without Direct Cooperativity.

Journal of chemical theory and computation·2026
Same author

Large Data Set Analysis Reveals Structural Origin of Peptide Collisional Cross Section Bimodal Behavior.

Journal of the American Society for Mass Spectrometry·2025
Same author

Structure and function of otoferlin, a synaptic protein of sensory hair cells essential for hearing.

Science advances·2025

Related Experiment Video

Updated: Jun 9, 2025

Analysis of SEC-SAXS data via EFA deconvolution and Scatter
10:59

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

9.0K

Bayesian electron density determination from sparse and noisy single-molecule X-ray scattering images.

Steffen Schultze1, Helmut Grubmüller1

  • 1Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen, Germany.

Science Advances
|October 25, 2024
PubMed
Summary

We developed a Bayesian method to determine biomolecular structures from single molecule X-ray scattering data. This approach overcomes low photon counts and high noise, enabling electron density determination for small proteins.

More Related Videos

Author Spotlight: Optimizing Cryo-EM Analysis with CryoSieve for Enhanced Particle Selection Efficiency
06:41

Author Spotlight: Optimizing Cryo-EM Analysis with CryoSieve for Enhanced Particle Selection Efficiency

Published on: May 10, 2024

1.5K
High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy
15:13

High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy

Published on: July 25, 2014

11.4K

Related Experiment Videos

Last Updated: Jun 9, 2025

Analysis of SEC-SAXS data via EFA deconvolution and Scatter
10:59

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

9.0K
Author Spotlight: Optimizing Cryo-EM Analysis with CryoSieve for Enhanced Particle Selection Efficiency
06:41

Author Spotlight: Optimizing Cryo-EM Analysis with CryoSieve for Enhanced Particle Selection Efficiency

Published on: May 10, 2024

1.5K
High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy
15:13

High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy

Published on: July 25, 2014

11.4K

Area of Science:

  • Structural biology
  • Biophysics
  • X-ray scattering

Background:

  • Single molecule X-ray scattering experiments using free-electron lasers (FELs) offer potential for high-resolution biomolecular structure determination.
  • Current limitations include low photon counts, high noise, and low hit rates, hindering electron density determination, especially for small molecules.
  • Existing methods primarily focus on larger specimens like viruses due to sufficient photon scattering for orientation determination.

Purpose of the Study:

  • To develop a rigorous computational approach to overcome limitations in single molecule X-ray scattering.
  • To enable electron density determination for small biomolecules, such as proteins, which suffer from low signal-to-noise ratios.
  • To account for various experimental complexities including intensity fluctuations, beam polarization, detector imperfections, and background scattering.

Main Methods:

  • A rigorous Bayesian approach was developed to analyze single molecule X-ray scattering data.
  • The method incorporates advanced corrections for intensity fluctuations, beam polarization, detector geometry, and incoherent/background scattering.
  • The approach was validated using synthetic scattering images and published virus data.

Main Results:

  • Demonstrated the feasibility of electron density determination for small proteins in an extreme high-noise Poisson regime.
  • Achieved detector-limited resolution of 9 nm on published virus data.
  • Required only 0.01% of the available photons per image for analysis of virus data, showcasing significant photon efficiency.

Conclusions:

  • The developed Bayesian method significantly enhances the capability of single molecule X-ray scattering for structural biology.
  • This approach paves the way for high-resolution structural studies of small biomolecules previously inaccessible with this technique.
  • The method's efficiency and robustness offer a promising path towards routine electron density determination from FEL X-ray scattering data.