In the first step of crystallization screening, the protein is exposed to a wide variety of reagents at different concentrations. Once a “hit” deemed to be conducive to crystallization is identified, parameters such as precipitant concentration, pH, and temperature are used to produce crystals suitable for analysis by X-ray diffraction. Crystals, crystalline precipitate, and phase separation are usually considered leads that are worth pursuing. Clear drops are mostly disregarded. This paper presents a screening technique that makes use of clear drops. Clear drops are subjected to evaporation with the aim of driving them to supersaturation. The findings reported bring a new dimension to screening and open up the scope for utilizing a potential wealth of crystallization conditions that are currently being ignored. Furthermore, this technique enables the utilization of far less protein sample and allows us to obtain the hits in shorter times.