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 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...

You might also read

Related Articles

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

Sort by
Same author

Structures of Cas9-Bound Double-Stranded DNA Mini-Circle Reveal Impacts of DNA Shape on Cas9 Target Interrogation.

bioRxiv : the preprint server for biology·2026
Same author

Cryo-EM Structure of a 95-Basepair Double-Stranded DNA Minicircle at 5.3 Å Resolution.

bioRxiv : the preprint server for biology·2026
Same author

Molecular mechanisms for subtype selectivity of kinin receptors' antagonists.

Nature communications·2026
Same author

ABEL-FRET bridges the timescale gap in single-molecule measurements of the structural dynamics in the A<sub>2A</sub> adenosine receptor.

Communications chemistry·2026
Same author

Structural and dynamic insights into agonist recognition and function of the thromboxane A<sub>2</sub> receptor.

Nature communications·2026
Same author

Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP.

Nature communications·2025

Related Experiment Video

Updated: Jul 10, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

Membrane protein crystallization in lipidic mesophases. A mechanism study using X-ray microdiffraction.

Vadim Cherezov1, Martin Caffrey

  • 1Department of Molecular Biology, The Scripps Research Institute, La Jolla CA 92037, USA.

Faraday Discussions
|October 25, 2007
PubMed
Summary

This study investigated membrane protein crystallization using the in meso method. Results show proteins migrate via a lamellar conduit, supporting the proposed mechanism for improved crystal growth.

More Related Videos

Crystallization of Membrane Proteins in Lipidic Mesophases
11:53

Crystallization of Membrane Proteins in Lipidic Mesophases

Published on: March 28, 2011

Use of a Robot for High-throughput Crystallization of Membrane Proteins in Lipidic Mesophases
20:21

Use of a Robot for High-throughput Crystallization of Membrane Proteins in Lipidic Mesophases

Published on: September 1, 2012

Related Experiment Videos

Last Updated: Jul 10, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

Crystallization of Membrane Proteins in Lipidic Mesophases
11:53

Crystallization of Membrane Proteins in Lipidic Mesophases

Published on: March 28, 2011

Use of a Robot for High-throughput Crystallization of Membrane Proteins in Lipidic Mesophases
20:21

Use of a Robot for High-throughput Crystallization of Membrane Proteins in Lipidic Mesophases

Published on: September 1, 2012

Area of Science:

  • Structural biology
  • Biophysics
  • Crystallography

Background:

  • Determining membrane protein structure is crucial for understanding their function.
  • Macromolecular crystallography is the primary method for atomic-resolution structure determination.
  • Producing high-quality crystals is a significant bottleneck in structural biology.

Purpose of the Study:

  • To test the hypothesis that membrane proteins migrate via a lamellar conduit during in meso crystallization.
  • To elucidate the mechanism of protein transport within lipidic mesophases during crystallization.

Main Methods:

  • Utilized the in meso crystallization technique with lipidic cubic phases.
  • Employed a sub-micrometer X-ray beam to probe the crystal-mesophase interface.
  • Analyzed diffraction patterns at micrometer spatial resolution.

Main Results:

  • Observed characteristic diffraction from a lamellar phase at the interface of a growing crystal.
  • This diffraction pattern supports the proposed lamellar conduit mechanism.
  • Provided evidence for protein transport from the bulk mesophase to the crystal face.

Conclusions:

  • The in meso method likely facilitates membrane protein crystallization through lamellar conduits.
  • This finding advances our understanding of membrane protein crystallization techniques.
  • Supports the proposed mechanism for in meso crystallization of membrane proteins.