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Related Experiment Videos

Systematic variation in DNA length yields highly ordered repressor-operator cocrystals.

S R Jordan, T V Whitcombe, J M Berg

    Science (New York, N.Y.)
    |December 20, 1985
    PubMed
    Summary
    This summary is machine-generated.

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    Researchers crystallized the lambda repressor

    Area of Science:

    • Molecular Biology
    • Structural Biology
    • Biophysics

    Background:

    • The lambda repressor protein controls viral DNA replication.
    • Understanding repressor-operator interactions is crucial for gene regulation studies.

    Purpose of the Study:

    • To obtain high-resolution crystals of the lambda repressor's operator-binding domain complexed with its operator DNA.
    • To facilitate direct structural determination of repressor-operator recognition.

    Main Methods:

    • Crystallization screening with DNA fragments of varying lengths (17-23 base pairs).
    • X-ray diffraction analysis of the obtained crystals.

    Main Results:

    • Crystals containing the lambda repressor operator-binding domain and the lambda operator site OL1 were successfully grown.

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  • Optimal crystallization was achieved with a 20-base pair DNA fragment.
  • The crystals exhibit P2I space-group symmetry and diffracted to at least 2.5 A resolution.

    • Conclusions:

    • The developed crystal system provides a platform for high-resolution structural studies.
    • This will enable detailed insights into the molecular mechanisms of repressor-operator binding.