The apicomplexan parasiteToxoplasma gondiimust invade host cells to continue its lifecycle. It invades different cell types using an actomyosin motor that is connected to extracellular adhesinsviathe bridging protein fructose-1,6-bisphosphate aldolase. During invasion, aldolase serves in the role of a structural bridging protein, as opposed to its normal enzymatic role in the glycolysis pathway. Crystal structures of the homologousPlasmodium falciparumfructose-1,6-bisphosphate aldolase have been described previously. Here,T. gondiifructose-1,6-bisphosphate aldolase has been crystallized in space groupP22₁2₁, with the biologically relevant tetramer in the asymmetric unit, and the structure has been determinedviamolecular replacement to a resolution of 2.0 Å. An analysis of the quality of the model and of the differences between the four chains in the asymmetric unit and a comparison between theT. gondiiandP. falciparumaldolase structures is presented.