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Bacteriophage λ uses an elegantly regulated and highly directional site-specific DNA-recombination reaction to integrate and excise its genome. A critical regulator of this process is the phage-encoded excisionase (Xis) protein, which dramatically stimulates excision by orchestrating the assembly of a higher order nucleoprotein structure that excises the prophage. The Xis protein stabilizes this recombination intermediate by substantially altering the trajectory of viral DNA and by cooperatively interacting with the λ integrase (Int) protein. In an attempt to understand how Xis controls the directionality of bacteriophage λ recombination, co-crystals of the DNA-binding domain of Xis in complex with its binding site within the P-arm of the phage have been obtained using the hanging-drop vapor-diffusion method. Using sodium acetate as a precipitating reagent, the Xis–DNA complex crystallizes in space group C2, with unit-cell parameters a = 80.2, b = 72.7, c = 38.8 Å, β = 104.1°. These crystals diffract beyond 1.5 Å resolution and are well suited for structural analysis using X-ray crystallography.
Keywords: excisionase.

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