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 Experiment Videos

Perspective: A toolbox for protein structure determination in physiological environment through oriented, 2D ordered,

M Altissimo1, M Kiskinova1, R Mincigrucci1

  • 1Elettra Sincrotrone Trieste, S. S. 14 km 163, 34149 Trieste, Basovizza, Italy.

Structural Dynamics (Melville, N.Y.)
|April 22, 2017
PubMed
Summary

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

Time-Domain Extreme-Ultraviolet Diffuse Scattering Spectroscopy of Nanoscale Surface Phonons.

Physical review letters·2026
Same author

Amplification of Spontaneous Emission from Doubly Excited He Atoms.

Physical review letters·2025
Same author

Corrigendum to: "Extreme ultraviolet transient gratings: A tool for nanoscale photoacoustics" [Photoacoustics 29 (2023) 100453].

Photoacoustics·2025
Same author

Reliability of toxicokinetic modelling for PFAS exposure assessment in contaminated water in northern Italy.

Heliyon·2024
Same author

Morpho-chemical characterization of individual ancient starches retrieved on ground stone tools from Palaeolithic sites in the Pontic steppe.

Scientific reports·2023
Same author

Unexpected silicon localization in calcium carbonate exoskeleton of cultured and fossil coccolithophores.

Scientific reports·2023

This study introduces a novel method to determine protein structures by creating ordered 2D protein arrays on surfaces. This approach aims to overcome limitations in current techniques, enabling structure determination under physiological conditions.

Area of Science:

  • Structural Biology
  • Biophysics
  • Materials Science

Background:

  • Determining protein structures is crucial for understanding biological functions.
  • Current methods like X-ray crystallography and cryo-electron microscopy have limitations including radiation damage and crystallization difficulties.
  • X-ray free-electron lasers offer potential but face signal-to-noise challenges for single-molecule studies.

Purpose of the Study:

  • To develop a new methodology to overcome signal-to-noise and protein crystallization limits.
  • To enable protein structure determination under physiological conditions.
  • To advance the field of structural biology by providing a more versatile technique.

Main Methods:

  • Creation of ordered, two-dimensional protein arrays with defined orientation on a self-assembled monolayer.

Related Experiment Videos

  • Development of a flexible toolbox for assembling diverse proteins onto functionalized surfaces.
  • Consideration of a graphene cover layer for experiments in physiological conditions.

    • Main Results:

    • A novel methodology is proposed to enhance signal-to-noise ratios for diffraction patterns.
    • The approach addresses limitations associated with protein crystallization.
    • The proposed technique facilitates protein structure determination under conditions closer to their native environment.

    Conclusions:

    • The developed methodology has the potential to overcome significant challenges in protein structure determination.
    • This approach could broaden the scope of proteins amenable to structural analysis.
    • Future applications may include studying protein dynamics and interactions in near-physiological settings.