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Membrane Protein Nanocrystallography (NanoMem)
Date du début: 1 janv. 2013, Date de fin: 31 déc. 2016 PROJET  TERMINÉ 

Modern structural biology builds upon synergies between lab-bench scale science on the one hand and large scale research infrastructure on the other. NanoMem recognises the transformative opportunities that are created by current X-ray source and detector developments to impact strongly on membrane protein structure, a challenging sub-field of structural biology. We will exploit synchrotron based micro-focus X-ray beams to address challenging diffraction studies from small membrane protein crystals; and embrace the revolutionary possibilities created by X-ray Free Electron Lasers to deliver an entirely new regime of high-resolution serial femtosecond crystallography of membrane proteins.These developments will place heavy demands on motivated and highly-trained talent. The time is ripe for bringing young scientists into the loop. Nanomem will train the nucleus of a new community spread across Europe that widens the access and use of non-conventional methods to capture membrane protein structures at high resolution. Our interdisciplinary and intersectorial research training work programme incorporates membrane protein production, purification and crystallisation, micro and nano-crystal manipulation, micro-focus diffraction at synchrotron sources, nano-focus diffraction at X-ray free electron lasers, serial femtosecond crystallography, software development, drug design, and commercialisation of the most helpful innovations. On-site scientific training of nine ESRs and one ER with seamless industrial participation will be complemented with training in areas such as intellectual property, communication skills and scientific mentoring. The current major European effort in the construction of new brilliant X-ray sources has to be matched by an investment in nurturing the birth of a scientific community for its exploitation, pushing the limits of our understanding of membrane protein structural biology.



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