The E-MeP consortium is focused on solving the structures of membrane proteins. These proteins comprise over 30% of known proteomes and already constitute approximately 50% of pharmacological targets.
The heterologous production, purification and crystallisation of a library of bioinformatically-selected membrane proteins has been streamlined by elucidating the parameters responsible for success and failure at each of these key stages. In the process new technologies are being developed and commercialised to overcome existing bottlenecks peculiar to membrane protein structural genomics, which cannot be solved by existing methods. E-MeP supports the training of young scientists in these skills through its sister project E-MeP-Lab.
The E-MeP consortium has selected membrane protein targets, which are expressed, refolded or solubilised, purified and delivered for crystallisation trials, to generate new 3D structures of membrane proteins.
E-MeP coordinator, Roslyn Bill, discusses the background to membrane proteins, the necessity for membrane research, and the challenges and applications which may arise in the future.
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To date eleven crystal structures have been published and over 40 diffracting crystals have been produced.
The E-MeP consortium is developing new technologies and high-throughput methods to overcome bottlenecks in membrane protein structural genomics.