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

RSPS version 4.0: a semi-interactive vector-search program for solving heavy-atom derivatives.

S D Knight1

  • 1Uppsala Biomedical Center, Department of Molecular Biology, Box 590, S-751 24 Uppsala, Sweden. stefan@xray.bmc.uu.se

Acta Crystallographica. Section D, Biological Crystallography
|February 10, 2000
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

Donor strand complementation mechanism in the biogenesis of non-pilus systems.

Molecular microbiology·2002
Same author

Discovery of potent and selective phenylalanine derived CCR3 receptor antagonists. Part 2.

Bioorganic & medicinal chemistry letters·2001
Same author

Bacterial adhesins: structural studies reveal chaperone function and pilus biogenesis.

Current opinion in chemical biology·2000
Same author

Chaperone-assisted pilus assembly and bacterial attachment.

Current opinion in structural biology·2000
Same author

PapD-like chaperones and pilus biogenesis.

Seminars in cell & developmental biology·2000
Same author

X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli.

Science (New York, N.Y.)·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 program aids in interpreting Patterson functions, primarily for locating heavy atoms in difference Patterson maps. It also assists in identifying molecules with non-crystallographic symmetry near crystallographic axes.

Area of Science:

  • Crystallography
  • Structural Biology
  • Computational Chemistry

Background:

  • The Patterson function is crucial for determining atomic structures in crystallography.
  • Accurate identification of heavy-atom positions is essential for solving complex crystal structures.
  • Locating molecules with non-crystallographic symmetry presents unique challenges in structural analysis.

Purpose of the Study:

  • To present a novel program for the inspection and interpretation of the Patterson function.
  • To facilitate the identification of heavy-atom sites from difference Patterson maps.
  • To enable the localization of molecules exhibiting non-crystallographic symmetry.

Main Methods:

  • Development of a computational program for Patterson function analysis.

Related Experiment Videos

  • Implementation of vector-based methods for heavy-atom site identification.
  • Inclusion of options for handling crystallographic and non-crystallographic symmetry.

    • Main Results:

    • The program effectively aids in finding heavy-atom positions from difference Patterson maps.
    • The software can locate molecules with non-crystallographic symmetry under specific geometric conditions.
    • The program offers robust tools for verifying potential solutions and analyzing symmetry elements.

    Conclusions:

    • The described program provides a valuable tool for crystallographic structure determination.
    • It enhances the process of heavy-atom phasing and the analysis of complex molecular arrangements.
    • The program's flexibility supports diverse applications in structural biology and materials science.