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Synergy between synchrotons and free electron lasers in studying ion transport with serial crystallography

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On Tuesday the 13th of October 2020 Przemyslaw Nogly of the Swiss Federal Institute of Technology (ETH) in Zurich will give a seminar entitled Synergy between synchrotons and free electron lasers in studying ion transport with serial crystallography. The seminar is open to members of the Department, other academic staff, students and members of Collegio A Volta. It will be delivered in Aula A of the Golgi/Spallanzani building but will also be accessible online. Instructions for online access are available on the poster that can be downloaded here.

Ion pumping microbial rhodopsins are integral membrane proteins employing a common
7-transmembrane helices architecture to transport different ion types. The specific residue composition impacts the protein dynamics and transport mechanism.
Rhodopsins utilize retinal chromophore to harvest light energy for protein activation, which makes them an ideal target for pump-probe experiments. We employ serial crystallography to capture structural intermediates in “real-time” and at non-cryogenic temperatures. I will present a combination of the X-ray Free Electron Laser and more accessible synchrotron data, which provide complementary insights into protein dynamics and ion transport.

1. Weinert T et al., Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography (2019) Science 365, 61-65.
2. Nogly P et al., Retinal isomerization in bacteriorhodopsin captured by a femtosecond X-ray laser (2018) Science 361, 6398.

Przemyslaw Nogly is a young group leader at at Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zurich, Switzerland. His research has been focussing on the structural dynamics of transport proteins and involves the development of experimental methods at synchrotron and Free Electron Laser facilities. He was awarded an Ambizione career development grant by the Swiss National Science Foundation to study the molecular mechanism of transport in a chloride pumping rhodopsin.

Serial crystallography.  Courtesy of Marius Schmidt/ University of Wisconsin Milwaukee

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