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Alpha helical membrane proteins are the targets for many pharmaceutical drugs and play important roles in physiology and disease processes. In recent years, substantial progress has been made in determining their atomic structure using X-ray crystallography. However, a major bottleneck still remains; the identification of conditions that give crystals that are suitable for structure determination. Over the past 10 years we have been analysing the crystallisation conditions reported for alpha helical membrane proteins with the aim to facilitate a rational approach to the design and implementation of successful crystallisation screens. The result has been the development of MemGold, MemGold2 and the additive screen MemAdvantage. The associated analysis, summarised and updated in this chapter, has revealed a number of surprisingly successfully strategies for crystallisation and detergent selection.

Original publication




Journal article


Adv Exp Med Biol

Publication Date





61 - 72


Crystallisation, Detergent selection, Membrane protein, Screen development, Animals, Bacterial Proteins, Buffers, Chemical Precipitation, Crystallization, Crystallography, X-Ray, Detergents, Humans, Hydrogen-Ion Concentration, Membrane Proteins, Protein Structure, Secondary, Salts