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

Scanning Electron Microscopy01:07

Scanning Electron Microscopy

5.2K
A scanning electron microscope (SEM) is used to study the surface features of a sample by using an electron beam that scans the sample surface in a two-dimensional manner. Typically, areas between ~1 centimeter to 5 micrometers in width can be imaged. SEM can be used to image bacteria, viruses, tissues as well as larger samples like insects. Conventional SEM gives a magnification ranging from 20X to 30,000X and spatial resolution of 50 to 100 nanometers.
Fundamental Principles
Accelerated...
5.2K
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

2.7K
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...
2.7K
Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.0K
Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
4.0K
Overview of Microscopy Techniques01:22

Overview of Microscopy Techniques

14.5K
The early pioneers of microscopy opened a window into the invisible world of microorganisms. In 1830, Joseph Jackson Lister created an essentially modern light microscope. The 20th century saw the development of microscopes that leveraged nonvisible light, such as fluorescence microscopy that uses an ultraviolet light source and electron microscopy that uses short-wavelength electron beams. These advances significantly improved magnification, image resolution, and contrast. By comparison, the...
14.5K
Preparation of Samples for Electron Microscopy01:20

Preparation of Samples for Electron Microscopy

6.6K
To be visualized by an electron microscope, either transmission or scanning, biological samples need to be fixed (stabilized) so the electron beam does not destroy them and dried thoroughly (desiccated/dehydrated) so the vacuum does not affect them. Fixation needs to be done as quickly as possible because the sample properties will start changing as soon as it is removed from its natural environment. For example, in a tissue sample, the oxygen levels begin decreasing, causing an altered...
6.6K
X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

4.6K
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...
4.6K

You might also read

Related Articles

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

Sort by
Same author

It started off as a Cys, how did it end up like this? Identifying the extent of unmodelled oxidatively modified cysteines within the Protein Data Bank.

Acta crystallographica. Section D, Structural biology·2026
Same author

Targeted knockout of barley Ycf54 demonstrates its essential function in the Mg-protoporphyrin IX monomethyl ester cyclase involved in chlorophyll biosynthesis.

Hereditas·2026
Same author

Time-Resolved Resonant Inelastic X-ray Scattering Reveals How Orbital Symmetry Alignment Enables C-H Activation.

Journal of the American Chemical Society·2026
Same author

Mapping the effects of specific radiation damage and solvent radiolysis in buffers and crystals with online UV-Vis absorption spectroscopy.

Acta crystallographica. Section D, Structural biology·2026
Same author

Tracking polar solvation dynamics of a photoexcited organic chromophore with ultrafast X-ray scattering.

Nature communications·2026
Same author

Integrated structural dynamics uncover a new B<sub>12</sub> photoreceptor activation mode.

Nature·2026

Related Experiment Video

Updated: Dec 21, 2025

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

9.4K

Scanning electron microscopy as a method for sample visualization in protein X-ray crystallography.

Emma V Beale1, Anna J Warren1, José Trincão1

  • 1Life Science, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK.

Iucrj
|May 21, 2020
PubMed
Summary
This summary is machine-generated.

Scanning electron microscopy (SEM) can be used to visualize protein crystals for X-ray diffraction. SEM radiation does not impact the diffraction quality of protein crystals, supporting its use on specialized beamlines.

Keywords:
VMXm beamlinecryoEMmacromolecular crystallographymicrofocus X-ray diffractionradiation damagescanning electron microscopystructural biologyvisualization tools

More Related Videos

Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

9.4K
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

13.2K

Related Experiment Videos

Last Updated: Dec 21, 2025

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

9.4K
Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

9.4K
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

13.2K

Area of Science:

  • Macromolecular crystallography
  • Structural biology
  • Biophysics

Background:

  • Determining high-resolution protein structures from micro- or submicrometre-sized crystals is crucial for understanding protein function.
  • Challenges in producing large crystals necessitate methods for analyzing micro- and nanocrystals.
  • Large protein complexes and membrane proteins often yield only small crystals.

Purpose of the Study:

  • To evaluate the suitability of scanning electron microscopy (SEM) for visualizing protein crystals for X-ray diffraction.
  • To assess the impact of SEM radiation on the diffraction quality of protein crystals.
  • To validate the integrated use of SEM on the versatile macromolecular crystallography microfocus (VMXm) beamline.

Main Methods:

  • Cytoplasmic polyhedrosis virus polyhedrin protein crystals were cryocooled on electron microscopy grids.
  • Crystals were exposed to SEM radiation prior to X-ray diffraction data collection.
  • X-ray diffraction data were processed using DIALS to compare data quality.

Main Results:

  • No statistically significant difference in data quality was observed between crystals exposed and not exposed to SEM radiation.
  • SEM proved effective in visualizing and locating micro- and nanocrystals.
  • The study confirmed the feasibility of integrating SEM with X-ray diffraction beamlines.

Conclusions:

  • SEM is a suitable method for visualizing protein crystals for X-ray diffraction experiments.
  • SEM radiation does not adversely affect the diffraction quality of protein crystals.
  • The integration of SEM on the VMXm beamline enhances crystal characterization and data collection.