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Isolation and crystallization of lambda exonuclease.

J van Oostrum, J L White, R M Burnett

    Archives of Biochemistry and Biophysics
    |December 1, 1985
    PubMed
    Summary
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    Researchers purified lambda exonuclease, an enzyme involved in DNA recombination, for structural analysis. They determined it is a tetramer and successfully crystallized it for X-ray diffraction studies.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Structural Biology

    Background:

    • Lambda exonuclease is a deoxyribonuclease induced by bacteriophage lambda.
    • Mutations in its gene suggest a role in general recombination.
    • Understanding its structure is key to elucidating its function.

    Purpose of the Study:

    • To purify lambda exonuclease for X-ray crystallographic analysis.
    • To determine the quaternary structure and molecular mass of the enzyme.
    • To obtain suitable crystals for detailed structural studies.

    Main Methods:

    • Large-scale enzyme purification from heat-induced lambda lysogen.
    • Analytical ultracentrifugation and SDS-polyacrylamide gel electrophoresis for molecular characterization.

    Related Experiment Videos

  • X-ray diffraction studies including precession photography and birefringence tests.

    • Main Results:

    • Lambda exonuclease was purified to homogeneity.
    • The enzyme exists as a tetramer with a molecular mass of 107,000 Da.
    • Crystals exhibiting cubic symmetry (space group P4(1)32 or P4(3)32) were obtained, containing 24 tetramers per unit cell.

    Conclusions:

    • Lambda exonuclease has been successfully purified and characterized as a tetrameric protein.
    • The enzyme's ability to form well-ordered crystals suitable for X-ray diffraction has been demonstrated.
    • These findings provide a foundation for future high-resolution structural studies to understand its role in recombination.