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 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...
Determination of Crystal Structures01:29

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 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...
X-ray Imaging01:24

X-ray Imaging

German physicist Wilhelm Röntgen (1845–1923) was experimenting with electrical current when he discovered that a mysterious and invisible "ray" would pass through his flesh but leave an outline of his bones on a screen coated with a metal compound. In 1895, Röntgen made the first durable record of the internal parts of a living human: an "X-ray" image (as it came to be called) of his wife’s hand. Scientists worldwide quickly began their own experiments with X-rays, and by 1900, X-ray was widely...
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...

You might also read

Related Articles

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

Sort by
Same author

High-throughput in situ single particle X-ray imaging of dehydrating viral capsids.

Light, science & applications·2026
Same author

Single-Particle X-ray Scattering Reveals a High Local Supersaturation of Precursors as the Origin of CoO Assembly Formation.

The journal of physical chemistry letters·2026
Same author

Photoinduced twist and untwist of moiré superlattices.

Nature·2025
Same author

SPRING, an effective and reliable framework for image reconstruction in single-particle Coherent Diffraction Imaging.

npj computational materials·2025
Same author

Hierarchically ordered porous transition metal compounds from one-pot type 3D printing approaches.

Nature communications·2025
Same author

Direct Observation of the Exciton-Polaron in Single CsPbBr<sub>3</sub> Quantum Dots.

ACS nano·2025
Same journal

Long-term stabilization of intensity-difference squeezing from four-wave mixing in rubidium vapor.

Optics express·2026
Same journal

Robust 3D topography measurement of large-range high-aspect-ratio structures based on dual-domain statistical filtering in SD-OCT.

Optics express·2026
Same journal

Broadband transmissive terahertz metasurface for simultaneous quad-mode OAM multiplexing.

Optics express·2026
Same journal

Leveraging two-dimensional materials for high-sensitivity optical sensors: quasi-bound states in the continuum within hybrid metasurfaces.

Optics express·2026
Same journal

Resolution investigation for dual-spherical-wave optical scanning holographic microscopy: methods and performance.

Optics express·2026
Same journal

Robustness of parallel subnetwork-filtered diffractive deep neural networks.

Optics express·2026
See all related articles

Related Experiment Video

Updated: May 21, 2026

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect
06:42

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect

Published on: March 19, 2019

Solving structure with sparse, randomly-oriented x-ray data.

Hugh T Philipp1, Kartik Ayyer, Mark W Tate

  • 1Cornell University, Laboratory of Atomic and Solid State Physics, Ithaca, NY, USA. htp2@cornell.edu

Optics Express
|June 21, 2012
PubMed
Summary
This summary is machine-generated.

Researchers reconstructed biomolecular structures from extremely low-photon X-ray diffraction images. This novel method uses an expectation maximization algorithm to process aggregate data, enabling structural recovery even with minimal signal per frame.

More Related Videos

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

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

Published on: October 2, 2017

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

Related Experiment Videos

Last Updated: May 21, 2026

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect
06:42

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect

Published on: March 19, 2019

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

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

Published on: October 2, 2017

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

Area of Science:

  • Biophysics
  • X-ray Crystallography
  • Computational Imaging

Background:

  • Single-particle imaging at X-ray Free-Electron Lasers (XFELs) generates vast datasets of low-photon diffraction patterns from randomly oriented biomolecules.
  • Extracting structural information from these low-fluence images is challenging due to the sparse signal and unknown particle orientations.

Purpose of the Study:

  • To demonstrate the feasibility of reconstructing structural information from extremely low-fluence single-particle X-ray diffraction data.
  • To validate a computational method capable of handling data with minimal photons per frame.

Main Methods:

  • Utilized an expectation maximization algorithm to process aggregate low-fluence diffraction data.
  • Employed a randomly oriented 2D x-ray mask as a test object to simulate biomolecular imaging conditions.
  • Reconstruction was performed without prior knowledge of the object's structure or orientation.

Main Results:

  • Successfully reconstructed structural information from images averaging only 2.5 photons per frame.
  • Demonstrated that meaningful structural data can be recovered even when individual frames contain minimal photon counts.
  • The algorithm effectively handled the aggregate data, overcoming the limitations of extremely sparse individual measurements.

Conclusions:

  • The developed expectation maximization approach is highly effective for single-particle imaging at extreme low-photon limits.
  • This method significantly expands the potential of X-ray Free-Electron Laser experiments by enabling structural determination from previously unusable data.
  • The technique promises to redefine measurement scenarios for obtaining useful structural signals in various imaging applications.