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

Cholera toxin crystals suitable for x-ray diffraction

P B Sigler, M E Dryan, H C Kiuefer

    Science (New York, N.Y.)
    |September 23, 1977
    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

    Comparison of methods for the rapid recognition of cholera vibrios.

    Bulletin of the World Health Organization·2010
    Same author

    Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation.

    Structure (London, England : 1993)·2001
    Same author

    Environmental signals controlling production of hemagglutinin/protease in Vibrio cholerae.

    Infection and immunity·2001
    Same author

    Preparation of components of archaeal transcription preinitiation complex.

    Methods in enzymology·2001
    Same author

    Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A.

    Nature·2001
    Same author

    Cell science and protein crystal growth research for the International Space Station.

    Journal of cellular biochemistry·2000

    Large crystals of cholera toxin were successfully grown, enabling high-resolution structural analysis. The protein retained full biological activity after crystallization, confirming its integrity for further research.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Crystallography

    Background:

    • Cholera toxin is a critical virulence factor in Vibrio cholerae infections.
    • Understanding cholera toxin's structure is essential for developing targeted therapeutics.
    • Previous structural studies may have been limited by crystal quality or stability.

    Purpose of the Study:

    • To grow high-quality cholera toxin crystals suitable for X-ray structure determination.
    • To confirm the biological activity of the cholera toxin protein after crystallization.
    • To provide a foundation for high-resolution structural analysis of cholera toxin.

    Main Methods:

    • Crystallization of cholera toxin.
    • X-ray diffraction analysis of crystal dimensions, symmetry, and order.

    Related Experiment Videos

  • Assessment of crystal radiation resistance.
  • Biological activity assays on protein from dissolved crystals.

    • Main Results:

    • Large, well-ordered cholera toxin crystals with P21 symmetry were obtained.
    • Crystals exhibited high resistance to radiation, beneficial for X-ray studies.
    • One molecule (approx. 84,000 daltons) per asymmetric unit was observed.
    • Dissolved crystals yielded protein that retained full biological activity.

    Conclusions:

    • The grown cholera toxin crystals are suitable for high-resolution X-ray structure determination.
    • The crystallization process preserves the biological integrity and activity of cholera toxin.
    • This work facilitates detailed structural investigations of cholera toxin.