Klp61F sediments as a homotetramer.

Source was embryos of wild-type fly line; protein produced from endogenous gene.

Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus and insect cell system.

Klp61F sediments as a homotetramer.

Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus-infected Sf9 cell system.

The Klp61F BASS domain forms a bipolar homotetramer assembly, as determined by immunolabeling of tagged N- and/or C-termini and electron microscopy.

Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus-infected Sf9 cell system.

The Klp61F BASS domain (35 kDa) forms a tetrameric complex (estimated 149 kDa), as determined by analytical ultracentrifugation.

Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus-infected Sf9 cell system.

The Klp61F BASS domain (35 kDa) exists primarily as a tetramer (estimated at 138 kDa), as determined by mass spectrometry.

Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus-infected Sf9 cell system.

The Klp61F BASS domain (35 kDa) exists primarily as a tetramer (estimated 136 kDa size), as determined by native PAGE.

Klp61F motor domain fused to the BASS-XL domain, with or without the tail domain, forms a tetramer.

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

Klp61F BASS-XL domain forms dimeric coiled-coils.

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