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MUST2022 Conference- a great success!
New scientific highlights- by MUST PIs Wörner, Chergui, and Richardson
FELs of Europe prize for Jeremy Rouxel- “Development or innovative use of advanced instrumentation in the field of FELs”
Ruth Signorell wins Doron prizefor pioneering contributions to the field of fundamental aerosol science
New FAST-Fellow Uwe Thumm at ETH- lectures on Topics in Femto- and Attosecond Science
International Day of Women and Girls in Science- SSPh asked female scientists about their experiences
New scientific highlight- by MUST PIs Milne, Standfuss and Schertler
EU XFEL Young Scientist Award for Camila Bacellar,beamline scientist and group leader of the Alvra endstation at SwissFEL
Prizes for Giulia Mancini and Rebeca Gomez CastilloICO/IUPAP Young Scientist Prize in Optics & Ernst Haber 2021
Nobel Prize in Chemistry awarded to RESOLV Member Benjamin List- for the development of asymmetric organocatalysis
NCCR MUST at Scientifica 2021- Lightning, organic solar cells, and virtual molecules
#NCCRWomen- NCCR MUST celebrates 50 years women’s right to vote in Switzerland

Radiation Damage and Phasing in Protein Crystallography at X-ray Free-Electron Lasers

Date Di, 15.03.2016 - Di, 15.03.2016
Time 13.15
Speaker Dr. Karol Nass, Max-Planck-Institut, Heidelberg, Germany
Location OSGA/EG06 (Hörsaal PSI Schulungsgebäude)
Program Abstract
The ultrafast radiation damage process begins with photoionization, followed by impact ionization by photo- and Auger electrons. The ionization of atoms develops with time, ultimately causing lattice disorder and Coulomb explosion of the crystal. Due to very short pulse duration, it has been proposed that diffraction can be recorded before significant structural changes occur. This has been termed “diffraction-before-destruction”. However, achieving sufficient scattering signal for measuring nanocrystals or non-crystalline single particles requires higher power densities than those used in microcrystallography experiments.
In order to explore whether undamaged crystal structures can be obtained with higher power densities at the sample, we used two colour x-ray FEL pulses (15 fs) with variable (0-100fs) time delay from the Linac Coherent Light Source (LCLS). These pulses were focused to approximately 100 nm2 to study radiation damage processes in protein crystals in a time-resolved fashion.
It is expected that a significant fraction of atoms in the crystal become highly ionized during exposure to the tightly focused x-ray FEL pulse. Indications of global and specific radiation damage and observation of correlated movement of atoms in the structure will be discussed. In addition, de novo phasing approaches and efforts in minimizing the systematic errors will be discussed.

1Karol Nass, 2Sébastien Boutet, 2Andrew Aquila, 1Thomas R.M. Barends, 1R. Bruce Doak, 1Lutz Foucar, 1Mario Hilpert, 2Mark S. Hunter, 2Jason Koglin, 1Gabriela Kovacsova, 2Mengning Liang, 1Christopher M. Roome, 1Robert L Shoeman, 1Ilme Schlichting

1Max-Planck-Institut für Medizinische Forschung, Jahnstraße 29, 69120 Heidelberg, Germany
2Linac Coherent Light Source, SLAC National Accelerator Laboratory, Sand Hill Road, Menlo Park, CA, 94025, USA
Download 160315 Invitation SwissFEL Seminar (101 KB)
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