Even in the absence of a known ligand and an experimental protein structure, we can still use virtual screening with an AlphaFold 3D model of the protein. However, before that, we need to determine the protein’s drugability and identify a potential ligand-binding site. Assuming that we have access to a purified protein, we can also run a high-throughput screen (HTS) in combination with a biochemical assay or use NMR spectroscopy to screen a fragment library. If the target protein’s experimental structure is unavailable, SARomics Biostructures provides custom gene-to-protein-structure services. In such cases, the protein is cloned, expressed, purified, and crystallized, and its X-ray crystallographic structure is determined. In addition, our library of FastLane structures is designed to accelerate our clients’ projects by offering over 600 proteins for co-crystallization with the client’s ligands, with a turnaround time of a few weeks.
