X-ray crystallography is the method of choice for solving the structure of molecules with the size up to 1 MDa, while most typical systems consist of ordered domain structures from few 100 kDa to peptides and small molecules. Crystallography is the most popular structural biology method in use. The main requirement is that your sample is ordered and pure enough to crystallize. Macromolecular crystallisation requires few milligran amounts of purified protein, and can yield higher resolution structures  than any other technique.

Robots are key to the expansion of macromolecular crystallography. They can accurately handle nanolitre volumes and so do the crystallisation experiments with only 5-10% of the protein required for manual setup. The small drops also equilibrate faster allowing faster analysis of the results.

For each 96-formatted screen, we ask you to provide 20 ul of the concentrated protein sample. We prepare the sample for the crystallisation, dispense all crystallisation solutions and the protein drops on the crystallisation plate, seal plates and image the experiment. You will get an access to the a viewer program (PiXray)  to look at the images and the history of each drop.