Nuclear extract was fractionated through several different chromatographic steps, selecting for chromatin remodeling activity.

Iswi, Acf1, Chrac-14 and Chrac-16 interact as part of the approximately 670 kDa CHRAC complex.

Identity of CHRAC subunits determined in this and other publications by mass spectrometry (FBrf0129776, FBrf0138380).

Top2 later shown to be a contaminant that is not part of the CHRAC complex (FBrf0138380).

Source was embryonic nuclear extract of wild-type fly line; proteins produced from endogenous genes.

Iswi, Acf1, Chrac-14 and Chrac-16 interact as part of the approximately 660 kDa CHRAC complex.

Identity of CHRAC subunits determined in this and other publications by mass spectrometry (FBrf0097684, FBrf0129776) and confirmed by western blot.

Top2 later shown to be a contaminant that is not part of the CHRAC complex (FBrf0138380).

Source was embryonic nuclear extract of wild-type fly line; proteins produced from endogenous genes.

Nuclear extract was fractionated through several different chromatographic steps, selecting for chromatin remodeling activity.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced and labeled by in vitro translation.

The Chrac-14-Acf1 interaction is not affected by nuclease treatment, and is thus not due to indirect DNA-mediated interactions.

Source was cell extract of baculovirus-infected Sf9 cell line; bait produced from transfected construct; prey produced from transfected construct.

Acf1 and Chrac-14 were coexpressed with His-tagged Chrac-16.