I. Introduction
Modern pharmaceutical engineering often uses the physical protein structure to understand the interaction between a potential drug and its intended target. This structure can be obtained using X-ray crystallography. The basic process is described in [1] as follows. First, well-ordered crystals are nucleated and grown in individual containers under highly controlled conditions. Once mature, the crystals are removed from the growth medium (harvested), cryoprotected, and flash-cooled. Finally, the crystals are placed into an X-ray beam and their diffraction pattern is recorded and numerically analyzed to reconstruct the underlying physical structure. Due to the high demand of this technique, most of these steps have been both highly parallelized and automated. However, one of the most laborious processes, the actual harvesting of the crystals, is still performed manually.