Abstract

Medium-sized single crystals with near-to-perfect habits and no defects that produce well resolved and intense diffraction patterns are the dream of every protein crystallographer. Four basic crystallisation methods are available to grow such crystals. As half a century ago in chemistry labs, crystallisation assays can be set up using either (i) in batch, (ii) by the diffusion of vapour between hanging (or sitting) droplets and a reservoir of precipitant, (iii) by dialysis across a semi-permeable membrane or (iv) free interface diffusion at the interface of two liquids.

  In this seminar an overview of crystal growth methods using conventional and non-conventional experimental methods will be presented. In order to control the kinetics of the crystallisation process, control of physical and chemical parameters allow us to control the nucleation, and crystal growth of biological macromolecules. Finally, a short overview of the main counter-diffusion methods and new strategies for enhancing the crystal quality for high resolution X-ray crystallography will be also revised.