Abstract
A combined imaging and dynamic light scattering (DLS) system has been developed for routine measurements in droplets in the multiwell plates used in protein crystallization. The system was tested with several standard proteins and found to be of high value for rapid identification of good crystallization conditions. A relationship between the rate of protein-aggregate-size increase and the probability of crystal formation was observed. DLS is a suitable tool for a fast optimization of the protein crystallization process.
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