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Affinity copurification of VP13/14 and pUL17. Hep2 cells were infected with either HSV-1(F) or a recombinant HSV-1 bearing a histidine tag fused to the C terminus of pUL17. Lysates of the cells were clarified, and soluble proteins were subjected to affinity chromatography on Ni2+-containing beads. After extensive washing, proteins bound to the beads were eluted in SDS, electrophoretically separated, and subjected to immunoblotting with antibodies to pUL17 (A) or VP13/14 (B).
