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

Likelihood-enhanced fast rotation functions.

Laurent C Storoni1, Airlie J McCoy, Randy J Read

  • 1Department of Haematology, University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, England.

Acta Crystallographica. Section D, Biological Crystallography
|March 3, 2004
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

Scotty: lattice coincidences for macromolecular crystallographic phasing.

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

Scotty: lattice coincidences in the Protein Data Bank.

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

AlphaFold as a prior: experimental structure determination conditioned on a pretrained neural network.

Nature methods·2026
Same author

Xtricorder: a likelihood-enhanced self-rotation function and application to a machine learning-enhanced Matthews prediction of asymmetric unit copy number.

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

Structure of Bovine Glycine <i>N</i>-Acyltransferase Clarifies Its Catalytic Mechanism.

Biochemistry·2025
Same author

Model Quality Assessment for CASP16.

Proteins·2025
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

Maximum-likelihood rotation targets improve molecular replacement accuracy but are computationally intensive. New likelihood-enhanced targets, computed rapidly using fast Fourier transforms, offer improved sensitivity and efficiency in protein structure determination.

Area of Science:

  • Structural biology
  • Computational crystallography

Background:

  • Traditional rotation targets in molecular replacement (MR) are less sensitive to correct orientation.
  • Brute-force searches using maximum-likelihood targets are computationally expensive, requiring hours to days.

Purpose of the Study:

  • To develop computationally efficient and sensitive rotation targets for molecular replacement.
  • To improve the speed and accuracy of determining correct molecular orientation in crystallographic studies.

Main Methods:

  • Developed series approximations to the full maximum-likelihood target.
  • Implemented fast Fourier transforms (FFTs) for rapid computation of these approximations.
  • Integrated likelihood-enhanced targets into the Phaser program.

Related Experiment Videos

Main Results:

  • Likelihood-enhanced targets are significantly more sensitive to correct orientation than traditional methods like the Crowther fast rotation function.
  • These targets leverage information from partial solutions, further enhancing accuracy.
  • Computation time is reduced from hours/days to minutes.

Conclusions:

  • Likelihood-enhanced rotation targets provide a computationally feasible and more sensitive approach for molecular replacement.
  • Phaser now incorporates these improved targets, accelerating protein structure determination.