The high-throughput crystallization laboratory at HWI houses state-of-the-art facilities for screening conditions suitable to grow the high quality single crystals required for molecular structure determination by X-ray diffraction. As currently configured, the lab has the capacity to evaluate as many as 200 new samples each month. A large number of experiments (1536) can be set up within minutes after a protein sample is received, thereby reducing the chance for protein degradation.

The approach used for screening growth conditions is to incubate, under paraffin oil, small aqueous aliquots of the sample protein with chemical mixtures (called ‘cocktails’) that are designed to induce a state of supersaturation. The protein molecules will then be driven out of solution and, under proper conditions, crystals will form. In the high-throughput lab, screening experiments are conducted in microassay plates using the distinct cocktails containing varying precipitants.

The high-throughput experiments are set up using pipetting robots. Two custom-made reader tables are used to document the results with a digital camera. The digital images are automatically transferred to a storage system, and the plates are stored in temperature-controlled incubators. Once initial crystallization conditions are identified, they are fine-tuned with additional experiments. The crystallization lab contains all the equipment needed to optimize crystal size and quality.