Abstract
X-ray crystallography is an important technique for structure-based drug discovery, mainly because it is the only technique that can reveal whether a ligand binds to the target protein as well as where and how it binds. However, ligand screening by X-ray crystallography involves a crystal soaking experiment, which is usually performed manual. Thus, the throughput is not satisfactory for screening large numbers of candidate ligands. In this study, we developed a technique to anchor protein crystals to mounting loops by using gel and inkjet technology; the method allows soaking of the mounted crystals in ligand-containing solution. This new technique may assist in designing a fully automated drug screening pipeline.
