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Biocrystallogenesis of RNA - protein systems


The preparation of high quality crystals in order to determine three-dimensional structures of biological macromolecules is the major bottleneck of x-ray crystallography studies. This project deals with biocrystallogenesis and its goal is to provide strategies and practical methods to facilitate the preparation and the optimisation of macromolecular crystals. A foreseen consequence of this approach is a faster access to structural data. The targets are aminoacyl-tRNA synthetases and transfert RNAs (tRNA) that are key actors in the translation of genetic information. These macromolecules are of immediate biological interest for the host laboratory. Indeed, their 3D structures are indispensable for a better understanding of the tRNA aminoacylation reaction. Further, the recent discovery of a link between structural alterations in such systems and human pathologies enhances this interest.

The project is multidisciplinary and involves bio-computing (to create a dedicated database in order to follow and compare crystallization assays), biochemistry and molecular biology (for cloning, expression and purification of targets), physical-chemistry of crystallization (to establish phase diagrams, to crystallize the targets in gelified media, to control the growth of their crystals by temperature or pressure variation,...) and physics (to evaluate crystal quality and perfection by x-ray diffraction and topography).

The project will benefit from long lasting expertise of the host laboratory and associated biology groups, an d from experience in structural biology and biocomputing acquired by the proposer during his Marie Curie training period. The attribution of an ERG would encourage the first step of the proposer and apos;s career after his reintegration. It would also rein force the development of an infrastructure for applied biocrystallogenesis at the host institute with a more general interest in the context of structural genomics prospective in the European Research Area.

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