000407959 001__ 407959
000407959 005__ 20230212180953.0
000407959 0247_ $$2CORDIS$$aG:(EU-Grant)801406$$d801406
000407959 0247_ $$2CORDIS$$aG:(EU-Call)H2020-FETOPEN-1-2016-2017$$dH2020-FETOPEN-1-2016-2017
000407959 0247_ $$2originalID$$acorda__h2020::801406
000407959 035__ $$aG:(EU-Grant)801406
000407959 150__ $$aMass Spectrometry for Single Particle Imaging of Dipole Oriented protein Complexes$$y2018-09-01 - 2023-06-30
000407959 371__ $$aHEINRICH-PETTE INSTITUT LEIBNIZ INSTITUT FUER EXPERIMENTELLE VIROLOGIE$$bHPI$$dGermany$$ehttp://www.hpi-hamburg.de$$vCORDIS
000407959 371__ $$aFASMATECH EPISTIMONIKI KAI TECHNOLOGIKI ANONYMI ETAIREIA$$bFASMATECH SCIENCE & TECHNOLOGY SA$$dGreece$$ehttp://www.fasmatech.com$$vCORDIS
000407959 371__ $$aSPECTROMETRY VISION BV$$bMS VISION$$dNetherlands$$ehttp://www.msvision.eu$$vCORDIS
000407959 371__ $$aUppsala University$$bUppsala University$$dSweden$$ehttps://www.uu.se/en/$$vCORDIS
000407959 371__ $$aUniversity of Manchester$$bUniversity of Manchester$$dUnited Kingdom$$ehttp://www.manchester.ac.uk/$$vCORDIS
000407959 371__ $$aUNI: Université de Claude Bernard   Lyon F$$dFrance$$ehttp://www.univ-lyon1.fr/$$vCORDIS
000407959 371__ $$aEuropean X-Ray Free Electron Laser$$bEuropean X-Ray Free Electron Laser$$dGermany$$ehttp://www.xfel.eu/$$vCORDIS
000407959 371__ $$aUniversity of Greifswald$$bUniversity of Greifswald$$dGermany$$ehttp://www.uni-greifswald.de/?L=1$$vCORDIS
000407959 372__ $$aH2020-FETOPEN-1-2016-2017$$s2018-09-01$$t2023-06-30
000407959 450__ $$aMS SPIDOC$$wd$$y2018-09-01 - 2023-06-30
000407959 5101_ $$0I:(DE-588b)5098525-5$$2CORDIS$$aEuropean Union
000407959 680__ $$aThe European XFEL has just entered user operation. With its unparalleled peak brilliance and repetition rate, European XFEL has the potential to further applications in single particle imaging (SPI), thus far limited to large viral particles at X-ray Free-Electron Lasers (XFEL). SPI will allow imaging protein complexes without the need for crystallization. This eventually renders transient conformational states accessible for high resolution structural studies yielding molecular movies of biomolecular machines. A major bottleneck is the wealth of data required to reconstruct a single structure leading to long processing times. This is currently also a problem in electron microscopy (EM).
MS SPIDOC will overcome this data challenge by developing a native mass spectrometry (MS) system for sample delivery, named X-MS-I. It will provide mass and conformation selected biomolecules, which are oriented along their dipole axis upon imaging. This will enable structural reconstruction from much smaller datasets speeding up the analysis time tremendously. Moreover, the system features low sample consumption and a controlled low background easing pattern identification.
The main objectives of the project are:
• Deliver mass and conformation separated biomolecules for SPI.
• Orient proteins for SPI.
• Image protein complex unfolding
• Exploit potential of protein orientation for other applications
The MS SPIDOC consortium combines internationally leading expertise in different fields relevant to the project: Instrument design and development, computer simulations as well as working with biomolecules in the gas phase and on SPI are combined to implement the novel sample environment at the next generation XFEL facility. New components and methods will be opened to the market and thereby strengthen the European Research Area (ERA) and industry. This early stage high-risk project will give rise to a new technology with major impact on how to derive structures of biomolecules.
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000407959 909CO $$ooai:juser.fz-juelich.de:850409
000407959 970__ $$aoai:dnet:corda__h2020::fad3d8f8d88ce9299bee7885015c210c
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000407959 980__ $$aCORDIS
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