Abstract
Higher throughput has been ever demanded in the state-of-the-art protein crystallography beamlines for applications such as the screening of drug targets in protein-ligand complex structures at room temperature. As a potential method to achieve an order of magnitude higher throughput, we explore capturing of ejected droplets by an acoustic levitator to remotely load single protein crystal samples to an acoustic levitation diffractometer at the Swiss Light Source synchrotron facility. The results from X-ray diffraction experiments support the feasibility of this method as a fully automated sample delivery for high-throughput serial crystallography experiments using the acoustic levitation.
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