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.

Chrac-14 and Chrac-16 interact as part of the CHRAC complex.

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.

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).

Two-hybrid system: yeast GAL4-BD/GAL4-AD

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

Chrac-14 and Chrac-16 were co-expressed in bacterial cells.

Chrac-14 and Chrac-16 interact with Iswi as part of the CHRAC complex.

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.

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.

Chrac-14 and Chrac-16 interact via their histone folds in a \'handshake\' structure. Unstrucutured N- and C-terminal tails protrude from the structure.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

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

Chrac-14 and Chrac-16 were co-expressed in bacteria.

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).

Two-hybrid system: yeast GAL4-BD/GAL4-AD

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).

Two-hybrid system: yeast GAL4-BD/GAL4-AD