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

Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

3.0K
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...
3.0K
Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.5K
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...
4.5K
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

10.3K
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
10.3K

You might also read

Related Articles

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

Sort by
Same author

C-terminal domain of the filamentous hemagglutinin FhaB is crucial for interaction of <i>Bordetella pertussis</i> with ciliated epithelial cells.

bioRxiv : the preprint server for biology·2026
Same author

Cryo-FIB Lift-Out and Electron Tomography Workflow for Bacteria-Nanopillar Interface Imaging Under Native Conditions: Investigating Dragonfly Inspired Bactericidal Titanium Surfaces.

Small methods·2026
Same author

Volume electron microscopy reveals bacterial endosymbiosis within host mitochondria.

Communications biology·2026
Same author

Author Correction: Pr and Pfr structures of plant phytochrome A.

Nature communications·2026
Same author

Energy metabolism and adaptation to hypoxia in the non-photosynthetic green alga Leontynka.

BMC biology·2026
Same author

Two types of axonal muscarinic acetylcholine receptors mediate formation of saliva cocktail in the tick Ixodes ricinus.

Nature communications·2026

Related Experiment Video

Updated: Mar 1, 2026

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

9.6K

Single-cell structural biology with intracellular electron crystallography.

Štěpánka Bílá1,2, Dominik Pinkas3, Krishna Khakurel4

  • 1Faculty of Science, University of South Bohemia in České Budějovice, České Budějovice, Czech Republic.

Nature Communications
|February 27, 2026
PubMed
Summary

High-resolution protein structures are now possible from single intracellular crystals using IncelluloED. This method combines intracellular crystallization with 3D electron diffraction, significantly reducing sample volume requirements.

More Related Videos

Electron Cryotomography of Bacterial Cells
14:23

Electron Cryotomography of Bacterial Cells

Published on: May 6, 2010

26.3K
Subnanometer-resolution Structural Determination of Hemagglutinin from Cryo-electron Tomography of Influenza Viruses
08:19

Subnanometer-resolution Structural Determination of Hemagglutinin from Cryo-electron Tomography of Influenza Viruses

Published on: November 7, 2025

878

Related Experiment Videos

Last Updated: Mar 1, 2026

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

9.6K
Electron Cryotomography of Bacterial Cells
14:23

Electron Cryotomography of Bacterial Cells

Published on: May 6, 2010

26.3K
Subnanometer-resolution Structural Determination of Hemagglutinin from Cryo-electron Tomography of Influenza Viruses
08:19

Subnanometer-resolution Structural Determination of Hemagglutinin from Cryo-electron Tomography of Influenza Viruses

Published on: November 7, 2025

878

Area of Science:

  • Structural Biology
  • Biophysics
  • Cryo-electron Microscopy

Background:

  • Intracellular crystallization offers an alternative to protein purification for structural studies.
  • Previous methods like serial X-ray crystallography (InCellCryst) required large sample volumes from many cells.
  • High-resolution structural data is often limited for proteins crystallizing in few cells.

Purpose of the Study:

  • To develop a method for high-resolution structural analysis from single intracellular crystals.
  • To overcome limitations of sample volume and cell number in previous techniques.
  • To enable structural biology studies in a "single-cell structural laboratory" setting.

Main Methods:

  • IncelluloED combines intracellular crystallization with in situ 3D electron diffraction.
  • Utilizes widely available cryo-electron microscopy tools.
  • Demonstrated on a microcrystal of HEX-1 protein from Magnaporthe grisea within an insect cell.

Main Results:

  • Achieved 1.9 Å resolution structure from a single microcrystal (~1.6 µm³).
  • This contrasts sharply with serial X-ray crystallography requiring >11 million µm³ for similar resolution.
  • Successfully obtained high-resolution data from just one crystal within one cell.

Conclusions:

  • IncelluloED significantly advances high-resolution structural biology by enabling single-cell analysis.
  • The method democratizes structural studies, making them accessible in standard laboratories.
  • Paves the way for a future of "single-cell structural laboratories".