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

Integration of macromolecular diffraction data.

A G Leslie1

  • 1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, England. andrew@mrc-lmb.cam.ac.uk

Acta Crystallographica. Section D, Biological Crystallography
|October 26, 1999
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

Structure of southern bean mosaic virus at 2.8 A resolution.

Nature·2009
Same author

The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase.

The EMBO journal·2001
Same author

Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis.

Cell·2001
Same author

The structure and nucleotide occupancy of bovine mitochondrial F(1)-ATPase are not influenced by crystallisation at high concentrations of nucleotide.

FEBS letters·2001
Same author

The rotary mechanism of ATP synthase.

Current opinion in structural biology·2000
Same author

How the multifunctional yeast Rap1p discriminates between DNA target sites: a crystallographic analysis.

Journal of molecular biology·2000
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

Accurate diffraction intensity evaluation is crucial. Profile fitting improves standard error estimates and handles challenging diffraction spots better than summation integration, based on Poisson statistics.

Area of Science:

  • Crystallography
  • Materials Science
  • X-ray Diffraction

Background:

  • Diffraction intensity evaluation is fundamental in X-ray diffraction analysis.
  • Two primary methods exist: summation integration and profile fitting.
  • Accurate intensity and error estimation are critical for structural determination.

Purpose of the Study:

  • To derive equations for evaluating diffraction intensities and their standard errors using Poisson statistics.
  • To compare the accuracy and advantages of summation integration versus profile fitting.
  • To quantify the improvement offered by profile fitting, especially concerning X-ray background noise.

Main Methods:

  • Derivation of equations for intensity and standard error calculation based on Poisson statistics.

Related Experiment Videos

  • Analysis of the contribution of X-ray background to standard error in both methods.
  • Evaluation of profile fitting for handling saturated and incompletely resolved diffraction spots.

    • Main Results:

    • Equations derived highlight the significant impact of X-ray background on standard error.
    • Profile fitting demonstrates a quantifiable improvement in accuracy over summation integration.
    • Profile fitting successfully estimates intensities for saturated reflections and resolves overlapping spots.

    Conclusions:

    • Profile fitting is a superior method for evaluating diffraction intensities and their standard errors.
    • The derived equations provide a framework for understanding error sources in diffraction data.
    • Profile fitting enhances data quality by addressing limitations of traditional summation integration.