Ligand-binding G Protein-Coupled Receptors naturally exist in several diverse conformations, which requires the receptors to be inherently flexible. This structural heterogeneity, in combination with their hydrophobic nature, makes solving GPCR structures technically challenging and requires long timelines and large investments with uncertain outcomes.
To date, only ~30 structures of the 800 member superfamily have been solved. Moreover, most receptors have only been crystallized with a single compound. Although critically important to structure-based drug design (SBDD), solving multiple co-crystal structures using different classes of compounds is rarely achieved and technically unpredictable.


Abilita Bio aims to facilitate crystallization of novel receptors, and importantly to enable the generation of co-crystal structures of the same target with multiple lead compounds through our EMPs™ Platform.