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Crystallization of the Arc repressor.

S R Jordan, C O Pabo, A K Vershon

    Journal of Molecular Biology
    |September 20, 1985
    PubMed
    Summary
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    Salmonella phage P22 Arc repressor protein was crystallized. This structural study provides insights into phage repressor protein crystallization and characterization for further research.

    Area of Science:

    • Structural biology
    • Molecular biology
    • Virology

    Background:

    • Arc is a repressor protein encoded by Salmonella phage P22.
    • Bacteriophage repressors play crucial roles in regulating viral gene expression and lysogeny.
    • Understanding the structure of phage repressors is key to deciphering their regulatory mechanisms.

    Purpose of the Study:

    • To crystallize the Arc repressor protein from Salmonella phage P22.
    • To determine the crystallographic parameters and diffraction quality of the Arc repressor crystals.
    • To lay the groundwork for future structural and functional analyses of the Arc repressor.

    Main Methods:

    • Crystallization of the Arc repressor protein using ammonium phosphate solution.
    • X-ray diffraction analysis to determine crystal space group and unit cell dimensions.

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  • Assessment of crystal diffraction resolution.

    • Main Results:

    • Arc repressor protein successfully crystallized from ammonium phosphate at pH 8.0.
    • Crystals belong to the space group P212121.
    • Unit cell dimensions were determined as a = 90.26 Å, b = 52.88 Å, and c = 47.58 Å.
    • The crystals diffracted X-rays to a resolution of 2.2 Å.

    Conclusions:

    • The successful crystallization and initial diffraction data provide a foundation for high-resolution structural determination of the Arc repressor.
    • This structural information will be valuable for understanding the molecular mechanisms of phage P22 repression.
    • The findings contribute to the broader field of bacteriophage structural biology and protein crystallography.