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

You might also read

Related Articles

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

Sort by
Same author

A New Method to Determine the Transmembrane Conformation of Substrates in Intramembrane Proteolysis by Deep-UV Resonance Raman Spectroscopy.

Methods in enzymology·2017
Same author

CYP24A1 Mutations in a Cohort of Hypercalcemic Patients: Evidence for a Recessive Trait.

The Journal of clinical endocrinology and metabolism·2015
Same author

STATISTICAL ANALYSIS OF CORTICAL MORPHOMETRICS USING POOLED DISTANCES BASED ON LABELED CORTICAL DISTANCE MAPS.

Journal of mathematical imaging and vision·2011
Same author

[Epigenetics and pseudohypoparathyroidism].

Pathologie-biologie·2009
Same author

Synthesis and characterization of SERS gene probe for BRCA-1 (breast cancer).

Faraday discussions·2006
Same author

The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state.

Journal of molecular biology·2004

Related Experiment Video

Updated: Apr 19, 2026

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography
09:23

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography

Published on: October 29, 2010

11.7K

Sparse and incomplete factorial matrices to screen membrane protein 2D crystallization.

R Lasala1, N Coudray1, A Abdine2

  • 1New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027, USA.

Journal of Structural Biology
|December 6, 2014
PubMed
Summary

Electron crystallography is key for membrane protein structure. New screening matrices accelerate the growth of 2D crystals, improving success rates for structure determination.

Keywords:
96-well formatElectron cryomicroscopyElectron crystallographyHigh-throughput screeningMembrane proteinMembrane protein reconstitutionTwo-dimensional (2D) crystal

More Related Videos

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

30.8K
From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

14.3K

Related Experiment Videos

Last Updated: Apr 19, 2026

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography
09:23

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography

Published on: October 29, 2010

11.7K
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

30.8K
From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
09:55

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

Published on: July 4, 2016

14.3K

Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • Electron crystallography is ideal for determining membrane protein structures within their native lipid bilayers.
  • Two-dimensional (2D) crystal formation is crucial but challenging, often limiting the technique's application.
  • Current screening methods for crystallization conditions are often limited in scope.

Purpose of the Study:

  • To analyze published 2D crystallization conditions for membrane proteins.
  • To develop improved screening strategies for membrane protein 2D crystallization.
  • To accelerate the structure determination of membrane proteins using electron crystallography.

Main Methods:

  • Analysis of published crystallization data for 12 β-barrel and 138 α-helical membrane proteins.
  • Design of novel sparse and incomplete factorial screening matrices based on successful conditions.
  • Application of these matrices to screen crystallization conditions for 16 different membrane proteins.

Main Results:

  • Successful identification of optimal crystallization conditions through data analysis.
  • Implementation of new screening matrices leading to over 1300 tested conditions.
  • Generation of diffracting 2D crystals for six membrane proteins, suitable for structure determination.

Conclusions:

  • The developed screening matrices show significant promise for enhancing the efficiency of membrane protein 2D crystallization.
  • This approach is expected to accelerate the structure determination of membrane proteins.
  • Optimized screening strategies are vital for advancing membrane protein structural biology.