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

Fast Fourier feature recognition.

K Cowtan1

  • 1Department of Chemistry, University of York, Heslington, York YO10 5DD, England. cowtan@yorvic.york.ac.uk

Acta Crystallographica. Section D, Biological Crystallography
|September 22, 2001
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

Shift-field refinement of macromolecular atomic models.

Acta crystallographica. Section D, Structural biology·2020
Same author

Structural barriers to scientific progress.

Acta crystallographica. Section D, Structural biology·2020
Same author

Features and development of Coot.

Acta crystallographica. Section D, Biological crystallography·2010
Same author

General quadratic functions in real and reciprocal space and their application to likelihood phasing.

Acta crystallographica. Section D, Biological crystallography·2000
Same author

Eigensystem analysis of the refinement of a small metalloprotein.

Acta crystallographica. Section D, Biological crystallography·2000
Same author

Error estimation and bias correction in phase-improvement calculations.

Acta crystallographica. Section D, Biological crystallography·1999
Same journal

Structural insights into the synthesis of FMN in prokaryotic organisms.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Native sulfur/chlorine SAD phasing for serial femtosecond crystallography.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Serial crystallographic analysis of protein isomorphous replacement data from a mixture of native and derivative microcrystals.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

The first crystal structure of the peptidase domain of the U32 peptidase family.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Structural characterization of a mitochondrial 3-ketoacyl-CoA (T1)-like thiolase from Mycobacterium smegmatis.

Acta crystallographica. Section D, Biological crystallography·2015
See all related articles

This study details a masked Fourier-based search function for interpreting crystallographic data. This method improves atomic model building, especially at low resolutions, by using statistical targets for protein fragment identification.

Area of Science:

  • Crystallography
  • Structural Biology
  • Computational Biology

Background:

  • Automatic interpretation of crystallographic data is crucial for determining atomic models.
  • Existing methods face challenges, particularly with low-resolution data.
  • Fourier-based approaches offer potential advantages for this task.

Purpose of the Study:

  • To discuss the application and optimization of a masked Fourier-based search function for crystallographic data interpretation.
  • To enhance the statistical significance and accuracy of atomic model building.
  • To develop methods for creating protein fragment libraries for automated structure determination.

Main Methods:

  • Utilizing a masked Fourier-based search function for data interpretation.

Related Experiment Videos

  • Implementing statistical significance through appropriate electron-density targets and weighting.
  • Developing methods for constructing a library of protein fragments.
  • Demonstrating methods with a statistical target for identifying helical fragments.

    • Main Results:

    • The masked Fourier-based search function shows benefits for automatic interpretation.
    • Improved results are achieved at low resolutions by incorporating statistical significance.
    • Methods for building a protein fragment library are presented.
    • A statistical target for identifying short helical fragments was successfully constructed.

    Conclusions:

    • The masked Fourier-based search function is a valuable tool for automated crystallographic data interpretation.
    • Statistical approaches enhance the reliability of atomic model building, particularly for low-resolution datasets.
    • The developed methods facilitate the creation of fragment libraries, aiding in structure determination.