Forthcoming Events

11.07.2022 - 15.07.2022, Celeste Hotel, on UCF main campus, Orlando, Florida
05.09.2022 - 09.09.2022, Iseolago hotel, Iseo, Italy.


MUST2022 Conference- succesfully concluded
New scientific highlights- by MUST PIs 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
Kick-Off dynaMENT Mentoring for Women in Natural Sciences- with Ursula Keller as plenary speaker

The making of a molecular movie

January 3, 2017

Time-resolved serial femtosecond crystallography (TR-SFX)

Bacteriorhodopsin (bR) is a membrane protein that harvests the energy content from light to transport protons out of the cell against a transmembrane potential. Nango et al. used time-resolved serial femtosecond crystallography at an x-ray free electron laser to provide 13 structural snapshots of the conformational changes that occur in the nanoseconds to milliseconds following photoactivation. These changes begin at the active site, propagate toward the extracellular side of the protein, and mediate internal protonation exchanges that achieve proton transport.
The authors used time-resolved difference absorption spectra from bR microcrystals suspended in a lipidic cubic phase matrix (see earlier highlight) to create a molecular movie of the events. Obtaining the recordings required examining around 2 million small protein crystal samples with the free electron laser SACLA in Japan. The FEL hits the samples with very short, powerful X-rays, capturing precise moments. "It’s like a strobe light," says Jörg Standfuss, a biophysicist and head of the serial crystallography research group. "Unlike a flashlight, it reveals flickers of motion in the dark." The ultrashort light pulses make it possible to record data before the samples are destroyed by the powerful X-rays. Thanks to the new SwissFEL facility at PSI in Würenlingen, which opened on 5 December 2016, researchers at Swiss higher education institutions no longer have to go halfway around the world to conduct their experiments

Figure. Structure and function of bacteriorhodopsin (bR).(A) Schematic illustrating retinal covalently bound to Lys216 through a protonated Schiff base (SB) in an all-trans and a 13-cis configuration. (B) Proton-exchange steps (arrows) achieving proton pumping by bR. The primary proton-transfer step is from the SB to Asp85 and corresponds to the spectroscopic L-to-M transition. (C) 2mFobs – DFcalc electron density for the bR active site in its resting conformation. Electron density (gray) is contoured at 1.3σ (σ is the root mean square electron density of the map). W400, W401, and W402 denote water molecules.

News items
Reference: Nango, E., A. Royant, M. Kubo, T. Nakane, C. Wickstrand, T. Kimura, T. Tanaka, K. Tono, C. Song, R. Tanaka, T. Arima, A. Yamashita, J. Kobayashi, T. Hosaka, E. Mizohata, P. Nogly, M. Sugahara, D. Nam, T. Nomura, T. Shimamura, D. Im, T. Fujiwara, Y. Yamanaka, B. Jeon, T. Nishizawa, K. Oda, M. Fukuda, R. Andersson, P. Båth, R. Dods, J. Davidsson, S. Matsuoka, S. Kawatake, M. Murata, O. Nureki, S. Owada, T. Kameshima, T. Hatsui, Y. Joti, G. Schertler, M. Yabashi, A.-N. Bondar, J. Standfuss, R. Neutze and S. Iwata (2016). A three-dimensional movie of structural changes in bacteriorhodopsin. Science 354: 1552 (10.1126/science.aah3497) Nango-2016 (1.52 MB).

Also see the the SNF Press Release

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