X-probe · Advanced XFEL and Synchrotron based Probes of Protein Structure and Dynamics
Horizon 2020 — Marie Skłodowska-Curie Actions
- Duration
- 2015-01-01 → 2018-12-31
- EU contribution
- €2,331,285
- Participants
- 11
- Scheme
- MSCA-ITN-ETN
Lines connect the coordinator with its partners.
Results in brief
Advanced XFEL and Synchrotron based Probes of Protein Structure and Dynamics
In the cross-disciplinary X-Probe project we have built upon the opportunities created by current X-ray sources and of the new ones recently made operative in Europe and worldwide. We have timely trained a new generation of scientists for the present generation of advanced X-ray facilities. Scientifically, X-probe has impacted on our understanding of protein conformational dynamics from femtoseconds to seconds, one of the most challenging problems in structural biology. We have unveiled the structural dynamics of protein that constitute relevant targets in pharmacology and nanotechnology. X-Probe has advanced the technological field of serial approaches at synchrotron radiation facilities by developing software and hardware solutions that extend the revolutionary possibilities created by X-ray Free Electron Lasers, which combine ultrafast X-ray pulses with high brilliance focusing capabilities. Exploitation of these changing technical capabilities required interdisciplinary collaboration between structural biologists, physical chemists, beamline engineers, software developers and industrial partners. Rapid changes in the state-of-the-art demanded young researchers to be trained to meet new experimental, technical and analysis challenges at the forefronts of structural biology. X-probe addressed this challenge through an interdisciplinary and intersectorial training network incorporating protein micro-crystallisation, sample manipulation, beamline development, micro-focus diffraction, software development, time-resolved diffraction, time-resolved wide angle X-ray scattering, and serial femtosecond crystallography. On-site scientific training and seamless industrial participation was complemented with a scientific mentoring program and training in areas such as strategic project planning, intellectual property, commercialisation and communication skills. We delivered a young team of motivated researchers trained to develop new tools for extracting new insights in protein structural dynamics from femtoseconds to second that exploit the extreme X-ray brilliance of recently developing X-ray user facilities. The very relevant European investments into the European XFEL and SwissFEL as well as the ongoing upgrade of synchrotron radiation sources demanded training of young scientists to fully exploit the scientific and technological avenues opened by this European and national effort, we developed a synergistic approach with technologically advanced enterprises to allow ESRs to convert knowledge and ideas into products and services for society and their own benefit.
Data: CORDIS, © European Union
Project objective
This cross-disciplinary Marie Curie Innovative Training Network builds upon the transformative opportunities created by existing X-ray sources and new sources soon to be operative in Europe. These opportunities include using ultrafast X-ray sources to extract time-dependent structural information from proteins; and revolutionary possibilities created by X-ray Free Electron Laser radiation for an entirely new regime of pre-damage serial femtosecond crystallography. No lag should exist between building new sources and training the next generation of scientists well versed in using these facilities. Our research training will yield new scientific insights on fundamental properties of protein structure and dynamics: one of the most challenging problems in structural biology; and technological advancements in diverse fields from pharmacology to nanotechnology. X-probe creates close interdisciplinary collaboration between structural biologists, physical chemists, beamline engineers, software developers, and industrial partners. The rapidly changing state-of-the-art demands that young researchers are trained to meet these new experimental, technical and analysis challenges at the forefront of structural biology and photochemistry. X-probe’s interdisciplinary and intersectorial training network incorporates four leading European X-ray facilities (ESRF, MAXIV Laboratory, European XFEL, SwissFEL); three academic laboratories at the forefront developing X-ray tools to probe protein dynamics; and both large and small industrial partners. Four principal scientists in X-probe are female. X-probe builds close cooperation between traditionally separate fields of research at the very cutting edge of structural biology and creates a visionary training network that would not be possible within any of the individual partner states.
Original text from CORDIS.
Participants
- UNIVERSITA DEGLI STUDI DI ROMA LA SAPIENZA · RomaCoordinatorItaly
- ASTRAZENECA AB · SodertaeljeSweden
- CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE CNRS · ParisFrance
- EUROPEAN SYNCHROTRON RADIATION FACILITY · GrenobleFrance
- GOETEBORGS UNIVERSITET · GoeteborgSweden
- LUNDS UNIVERSITET · LundSweden
- MOLIROM SRL · RomaItaly
- PAUL SCHERRER INSTITUT · VILLIGEN PSISwitzerland
- SAPIENZA INNOVAZIONE CONSORZIO · RomaItaly
- UNIVERSITY OF HAMBURG · HamburgGermany
- XTAL CONCEPTS GMBH · HAMBURGGermany
Links
- View on CORDIS
- DOI: 10.3030/637295
- http://www.x-probe.org
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e59ea84fdf&appId=PPGMS
- https://www.ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5afe0268d&appId=PPGMS
- https://www.ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5b02cfd6f&appId=PPGMS
- https://www.ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5b0d2a429&appId=PPGMS
- https://www.ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5b777f31c&appId=PPGMS
- https://www.ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5b7b5963c&appId=PPGMS
- https://www.ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5b89ebdcd&appId=PPGMS
- https://www.ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5c115c4e6&appId=PPGMS
- https://www.ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e5c22dcbb6&appId=PPGMS
Data: CORDIS, © European Union
