Protein Crystallisation

An important method for the determination of protein structures is x-ray analysis of protein crystals. The determination of the three-dimensional structure of proteins has contributed towards major advances in basic research, particularly in the fields of structural genomics and structure-based drug design. The most commonly used method for the crystallization of proteins is vapour diffusion which comprises both the sitting drop and hanging drop methods . One drop of protein solution is mixed with one drop of reagent solution and incubated together with a larger volume of reagent solution in a sealed well. Concentration gradients between the sample drop and the reservoir solution are balanced out by diffusion, which induces the crystallisation process if the correct conditions have been selected.
The microbatch method in which the sample drop is covered with oil is also widely used, and in this technique the choice of oil determines the rate of diffusion of the water in the sample drop through the oil. Numerous factors affect the crystallisation of proteins. Since the optimal crystallisation conditions generally cannot be predicted, a large number of attempts is often necessary in order to determine and optimise the appropriate conditions. Protein crystallisation therefore still represents a major bottleneck in structure analysis. The use of high-throughput technologies, such as pipetting robots and standardised microplates, makes it possible to test a large number of crystallization conditions in a short period of time and with relatively small amounts of protein.
The CrystalStar™ product range from Greiner Bio-One is a family of crystallisation plates and accessories designed specifically for high-throughput crystallization.