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

Crystals of the trp repressor-operator complex suitable for X-ray diffraction analysis.

A Joachimiak, R Q Marmorstein, R W Schevitz

    The Journal of Biological Chemistry
    |April 5, 1987
    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

    A funnel approach to enable analyses of epitope-specific human CD4 T cells specific for influenza and SARS-CoV-2.

    mBio·2026
    Same author

    Time-resolved β-lactam cleavage by L1 metallo-β-lactamase.

    Nature communications·2022
    Same author

    A novel signal transduction protein: Combination of solute binding and tandem PAS-like sensor domains in one polypeptide chain.

    Protein science : a publication of the Protein Society·2017
    Same author

    Insight into the sporulation phosphorelay: crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD.

    Protein science : a publication of the Protein Society·2013
    Same author

    Crystal structure of the novel PaiB transcriptional regulator from Geobacillus stearothermophilus.

    Proteins·2011
    Same author

    Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production.

    Proteins·2011

    High-resolution molecular images of trp repressor-operator complexes were obtained. Crystallization strategies for protein-DNA complexes remain challenging due to sensitivity to various factors.

    Area of Science:

    • Structural Biology
    • Biochemistry
    • Molecular Biology

    Background:

    • The trp repressor regulates gene expression by binding to the operator DNA sequence.
    • Understanding protein-DNA interactions at a molecular level is crucial for deciphering gene regulation mechanisms.

    Purpose of the Study:

    • To obtain high-resolution structural data of a simulated trp repressor-operator complex.
    • To investigate factors influencing the crystallization of protein-DNA complexes.

    Main Methods:

    • Crystallization of a simulated trp repressor-operator complex.
    • X-ray diffraction to determine molecular structure.
    • Analysis of crystal polymorphism and diffraction properties.

    Main Results:

    Related Experiment Videos

    • Obtained well-ordered crystals of the trp repressor-operator complex diffracting to better than 3-Å resolution.
    • Observed extensive crystal polymorphism sensitive to DNA length, terminal structure, and ion conditions.
    • Identified significant challenges in developing a consistent crystallization strategy.

    Conclusions:

    • High-resolution imaging of protein-DNA complexes is achievable but complex.
    • Crystallization protocols are highly sensitive to subtle changes in DNA and buffer conditions.
    • Further research is needed to establish reliable methods for protein-DNA complex crystallization.