Top2 dimerizes to form a complex with an apparent molecular mass of 660 kDa on gel filtration columns (greater than the predicted weight of 328 kDa).

Large Top2 oligomers were determined to be a contaminant of the similarly sized CHRAC complex preparations. Top2 and CHRAC are separable by hydroxyapatite chromatography.

Interaction in vitro; protein purified from wild type embryonic nuclear extract.

Nuclear extract was fractionated through several different chromatographic steps to obtain purified Top2, which was then subjected to gel filtration chromatography.

Interaction in vitro; protein produced as a recombinant fusion protein in yeast system.

Top2 dimerizes to form a complex with an apparent molecular mass of 340 kDa, as determined by multi-angle light scattering.