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[SA_scat] Interdisciplinary postdoc position in SAXS andbioinformatics at EMBL-Hamburg
- To: <sa_scat@iucr.org>
- Subject: [SA_scat] Interdisciplinary postdoc position in SAXS andbioinformatics at EMBL-Hamburg
- From: "Dmitri Svergun" <svergun@embl-hamburg.de>
- Date: Thu, 3 Feb 2011 14:31:31 +0100
- In-Reply-To: <20100220143318.23183zjd0e4952fy@webmail.embl-hamburg.de>
- References: <20100220143318.23183zjd0e4952fy@webmail.embl-hamburg.de>
Dear All, this is an announcement of the call for applications for EMBL Interdisciplinary Postdocs (EIPOD). The EIPOD positions are funded initially for three years and promote interdisciplinary research in biology. Attached below is a predefined EIPOD project in biological SAXS associated with the SAXS group in Hamburg. The application deadline is March, 20, 2011. The on-line application is available from http://www.embl.de/training/postdocs/eipod/ For further detail, please contact D.Svergun (Svergun@embl-hamburg.de) With best regards D. Svergun “Cross-validation of macromolecular models in solution built from small angle X-ray scattering” Coordinator: D.Svergun Partners: G.Kleywegt, A.-C. Gavin The project aims at the joint use of the bioinformatics and macromolecular crystallography (MX) to construct and validate the low resolution models obtained by small-angle X-ray scattering (SAXS). This technique experiences a renaissance in modern structural biology providing three-dimensional (3D) models based on the scattering data from solutions and being ideally suited for systemic studies of complex biological objects and networks. Recent progress in instrumentation (high brilliance synchrotrons) and novel data analysis approaches significantly enhanced the capabilities of SAXS in structural biology [1]. In particular, 3D shapes at a resolution of ca 1-2 nm can be reconstructed ab initio and quaternary structure of complexes can be modeled in terms of the high resolution models of the individual subunits. Building 3D models from SAXS is inherently ambiguous as the method provides low resolution information only. At present, objective criteria like crystallographic free R-factor and structural assessment tools like WHAT IF or CING are not present for SAXS-generated models. The validation of these models becomes an extremely important issue in view of the growing requests from the biological community to make these models available in the Protein Data Bank (PDB). The EIPOD will develop bioinformatic tools for a comprehensive validation of the SAXS models under the guidance of D.Svergun (EMBL Hamburg), developing advanced SAXS analysis methods [1]. The validation principles and approaches will be devised in collaboration with G. Kleywegt, (Head of PDBe, EBI Hinxton), an expert in the validation of protein models [2]. The EIPOD will be involved in the work of the wwPDB Task Force recently created to prepare conditions for inclusion of the SAXS models into PDB. The developed tools will be tested and applied to a challenging proteomics-scale project. The EIPOD will take part in preparation and SAXS analyses of the protein complexes selected from the ongoing biochemical screen in the A-C.Gavin’s group (EMBL Heidelberg), exploring new types of biological networks [3]. The combinatorial SAXS measurements will be performed utilizing a microfluidic device on a new high brilliance EMBL synchrotron beamline in Hamburg. The available high resolution structures of some complexes will be used to test the validation criteria. The latter will then be applied in the structural characterization of the complex formation in the entire interactome (hundreds of proteins) as a proof of principle of the validation approach. The research includes a synergistic use of structural, biochemical and bioinformatics methods, providing an excellent opportunity for a biologist, physicist or mathematician (preferably with bioinformatic, crystallographic or NMR background) to develop complementary skills during the work on this challenging and highly interdisciplinary project. 1. Mertens, H. D. T. & Svergun, D. I. (2010). Structural characterization of proteins and complexes using small-angle X-ray solution scattering. J Struct Biol 172, 128-141. 2. Kleywegt, G.J. (2007) Quality control and validation. Methods Mol Biol. 364, 255-272. 3. Kühner S., van Noort V., Betts M.J., Leo-Macias A., Batisse C., Rode M., Yamada T., Maier T., Bader S., Beltran-Alvarez P., Castaño-Diez D., Chen W.H., Devos D., Güell Cargol M., Norambuena T., Racke I., Rybin V., Schmidt A., Yus E., Aebersold R., Herrmann R., Böttcher B., Frangakis A.S., Russell R.B., Serrano L., Bork, P. & Gavin, A.C. (2009) Proteome organization in a genome-reduced bacterium. Science, 326, 1235-1240 _______________________________________________ sa_scat mailing list sa_scat@iucr.org http://scripts.iucr.org/mailman/listinfo/sa_scat
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