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

Overview and new developments in softer X-ray (2A < lambda < 5A) protein crystallography.

John R Helliwell1

  • 1Department of Chemistry, University of Manchester, Manchester M13 9PL, UK. john.helliwell@man.ac.uk

Journal of Synchrotron Radiation
|December 4, 2003
PubMed
Summary
This summary is machine-generated.

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

Miroslav Z. Papiz (1955-2026).

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

Crystallography in Open Science and its open educational resources.

Acta crystallographica. Section A, Foundations and advances·2026
Same author

50th anniversary of the Stanford SSRL synchrotron radiation and protein crystallography initiative.

Journal of synchrotron radiation·2026
Same author

Macromolecular crystallography for mammalian body temperature in support of molecular biophysics methods.

Biophysical reviews·2025
Same author

Towards patient-relevant structures: reviewing body-temperature biological macromolecules and their ligands for pharmaceutical applications.

Acta crystallographica. Section D, Structural biology·2025
Same author

Stephen Harrop (1966-2024).

Acta crystallographica. Section D, Structural biology·2025

Softer X-rays enhance protein crystallography by optimizing phase determination using anomalous scattering. This approach improves throughput and aids in future X-ray Free Electron Laser (XFEL) development for structural biology.

Area of Science:

  • Structural biology
  • Crystallography
  • X-ray diffraction

Background:

  • Development of new methodologies in structural biology utilizing synchrotron radiation and X-ray Free Electron Lasers (XFELs).
  • Exploration of softer X-ray wavelengths (2-3 Å) for enhanced phase determination in protein crystallography.

Purpose of the Study:

  • To describe recent trends in harnessing softer X-rays for phase determination in protein crystallography.
  • To demonstrate the optimization of anomalous scattering (f") using xenon L-edge and sulfur signals with softer X-rays.
  • To explore the potential of softer X-rays in advancing XFEL capabilities and single-particle imaging.

Main Methods:

  • Utilized softer X-rays (2 Å wavelength) to optimize anomalous scattering (f") at the xenon L1 absorption edge for Single Isomorphous Replacement Optimised Anomalous Scattering (SIROAS).

Related Experiment Videos

  • Determined protein hand using enhanced sulfur anomalous signal from disulphides.
  • Employed phase determination and improvement using optimized xenon L1-edge data and computational methods (CCP4 DM).

    • Main Results:

    • Successful structure determination of apocrustacyanin A1 using xenon L1-edge anomalous scattering.
    • Feasible auto-tracing of protein structure, with potential for improvement using tilted detector settings for back-scattering.
    • Optimization of synchrotron radiation beamline (SRS MPW MAD 10) for softer X-ray applications.

    Conclusions:

    • Softer X-rays (2-3 Å) significantly enhance protein crystallography throughput by optimizing anomalous scattering signals (xenon, iodine, sulfur).
    • Future XFEL development can benefit from softer X-ray wavelengths, potentially reducing complexity and cost.
    • The study supports the commencement of a new era in single-particle X-ray diffraction imaging.