Crystallisation of integral membranes requires milligrams of purified protein in a homogeneous, monodisperse state, and crucially, the membrane protein must also be fully functional and stable. The stability of membrane proteins in solution is dependent on the type of detergents used, but unfortunately the use of the most stabilising detergent can often decrease the probability of obtaining crystals that diffract to high resolution, especially of small membrane proteins. A number of strategies have been developed to facilitate the purification of membrane proteins in a functional form, which have led to new possibilities for structure determination.
