It is well established that aggregation of cell surface immunoglobulin is involved in signal transduction by cells of the immune system. It is less well understood what special properties of these cell surface aggregates are important in initiating the signal cascade. Several authors have proposed that cells respond to the size (Fewtrell and Metzger (1980) J. Immun. 125, 701-710) as well as the stereochemistry (Ortega et al. (1989) Eur. J. Immun. 19, 2251-2256) of receptor aggregates. One approach to arriving at data relevant to this question has been to construct simple bivalent ligands that can bind to surface immunoglobulin. Several authors have suggested that when these bivalent ligands interact with surface immunoglobulin the formation of small stable cyclic complexes is highly favored. In this paper we consider whether it is possible to completely determine the parameters that describe the binding of a bivalent ligand to a bivalent receptor with the available experimental technology. We show that with the appropriate analysis procedure, using a modified equivalent site model, these parameters can be reliably determined from only three experiments even when there is a large amount of ring formation.