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

Crystal structure of hexameric complex captured as 15 pairwise interactions.

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

Binding of Orc6 to preassembled Orc1-5 complex captured as 5 pairwise interactions.

Embryonic nuclear extract was treated with DNase and RNase.

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

Embryonic nuclear extract was treated with DNase and RNase.

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

His-Orc1, Orc2, Orc3, Orc4, Orc5 and MBP-Orc6 were co-infected, then purified by sequential His-Orc1 then MBP-Orc6 pull down with additional preparative gel filtration purification.

The Drosophila origin of replication complex (ORC) forms a stable, hexameric complex containing subunits Orc1, Orc2, Orc3, Orc4, Orc5 and Orc6.

Source was cell extract of baculovirus-infected High5 cell line; bait produced from transfected construct; prey produced from transfected construct.

The ORC complex visualized by EM was captured as 15 pairwise interactions. The addition of ATP caused the complex to adopt an active/open conformation.

Interaction in vitro; proteins produced as a recombinant fusion proteins in baculovirus and High5 cell system.

Comparison of EM structures of ORC complex, ORC complex bound to DNA and a ternary complex consisting of ORC, DNA and Cdc6 curated as a series on binary protein-protein interactions.

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