Zobrazeno 1 - 10
of 91
pro vyhledávání: '"Karol Nass"'
Autor:
Maximilian Wranik, Michal W. Kepa, Emma V. Beale, Daniel James, Quentin Bertrand, Tobias Weinert, Antonia Furrer, Hannah Glover, Dardan Gashi, Melissa Carrillo, Yasushi Kondo, Robin T. Stipp, Georgii Khusainov, Karol Nass, Dmitry Ozerov, Claudio Cirelli, Philip J. M. Johnson, Florian Dworkowski, John H. Beale, Scott Stubbs, Thierry Zamofing, Marco Schneider, Kristina Krauskopf, Li Gao, Oliver Thorn-Seshold, Christoph Bostedt, Camila Bacellar, Michel O. Steinmetz, Christopher Milne, Jörg Standfuss
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Abstract Serial crystallography at X-ray free-electron lasers (XFELs) permits the determination of radiation-damage free static as well as time-resolved protein structures at room temperature. Efficient sample delivery is a key factor for such experi
Externí odkaz:
https://doaj.org/article/f224092cc9184c46b2af0e3942817cf2
Autor:
Maximilian Wranik, Tobias Weinert, Chavdar Slavov, Tiziana Masini, Antonia Furrer, Natacha Gaillard, Dario Gioia, Marco Ferrarotti, Daniel James, Hannah Glover, Melissa Carrillo, Demet Kekilli, Robin Stipp, Petr Skopintsev, Steffen Brünle, Tobias Mühlethaler, John Beale, Dardan Gashi, Karol Nass, Dmitry Ozerov, Philip J. M. Johnson, Claudio Cirelli, Camila Bacellar, Markus Braun, Meitian Wang, Florian Dworkowski, Chris Milne, Andrea Cavalli, Josef Wachtveitl, Michel O. Steinmetz, Jörg Standfuss
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Photopharmacology manipulates the biological activity of small molecules by light. Using an X-ray laser, the authors follow the release of the drug azo-combretastatin A4 from tubulin and the concomitant structural changes over nine orders of magnitud
Externí odkaz:
https://doaj.org/article/31ccc9f5c1c7420b8b23b5fa45bdc9ee
Autor:
Stephen M. Keable, Adrian Kölsch, Philipp S. Simon, Medhanjali Dasgupta, Ruchira Chatterjee, Senthil Kumar Subramanian, Rana Hussein, Mohamed Ibrahim, In-Sik Kim, Isabel Bogacz, Hiroki Makita, Cindy C. Pham, Franklin D. Fuller, Sheraz Gul, Daniel Paley, Louise Lassalle, Kyle D. Sutherlin, Asmit Bhowmick, Nigel W. Moriarty, Iris D. Young, Johannes P. Blaschke, Casper de Lichtenberg, Petko Chernev, Mun Hon Cheah, Sehan Park, Gisu Park, Jangwoo Kim, Sang Jae Lee, Jaehyun Park, Kensuke Tono, Shigeki Owada, Mark S. Hunter, Alexander Batyuk, Roland Oggenfuss, Mathias Sander, Serhane Zerdane, Dmitry Ozerov, Karol Nass, Henrik Lemke, Roman Mankowsky, Aaron S. Brewster, Johannes Messinger, Nicholas K. Sauter, Vittal K. Yachandra, Junko Yano, Athina Zouni, Jan Kern
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
Abstract Photosystem I (PS I) has a symmetric structure with two highly similar branches of pigments at the center that are involved in electron transfer, but shows very different efficiency along the two branches. We have determined the structure of
Externí odkaz:
https://doaj.org/article/08b51738551f492bbef4bdd046b9396c
Autor:
Karol Nass, Camila Bacellar, Claudio Cirelli, Florian Dworkowski, Yaroslav Gevorkov, Daniel James, Philip J. M. Johnson, Demet Kekilli, Gregor Knopp, Isabelle Martiel, Dmitry Ozerov, Alexandra Tolstikova, Laura Vera, Tobias Weinert, Oleksandr Yefanov, Jörg Standfuss, Sven Reiche, Christopher J. Milne
Publikováno v:
IUCrJ, Vol 8, Iss 6, Pp 905-920 (2021)
Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) enables essentially radiation-damage-free macromolecular structure determination using microcrystals that are too small for synchrotron studies. However, SFX experiments o
Externí odkaz:
https://doaj.org/article/ad50bebd17b6464fb70fffcb3373aa32
Autor:
Marie Luise Grünbein, Alexander Gorel, Lutz Foucar, Sergio Carbajo, William Colocho, Sasha Gilevich, Elisabeth Hartmann, Mario Hilpert, Mark Hunter, Marco Kloos, Jason E. Koglin, Thomas J. Lane, Jim Lewandowski, Alberto Lutman, Karol Nass, Gabriela Nass Kovacs, Christopher M. Roome, John Sheppard, Robert L. Shoeman, Miriam Stricker, Tim van Driel, Sharon Vetter, R. Bruce Doak, Sébastien Boutet, Andrew Aquila, Franz Josef Decker, Thomas R. M. Barends, Claudiu Andrei Stan, Ilme Schlichting
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
X-ray fee-electron lasers (XFELs) enable time-resolved crystallography experiments and the structure determination of proteins with little or no radiation damage. However currently it is unknown whether the designated 4.5 MHz maximum pulse rate for t
Externí odkaz:
https://doaj.org/article/b9fa088215e4467aa2714fbb4e537fb1
Autor:
Karol Nass, Robert Cheng, Laura Vera, Aldo Mozzanica, Sophie Redford, Dmitry Ozerov, Shibom Basu, Daniel James, Gregor Knopp, Claudio Cirelli, Isabelle Martiel, Cecilia Casadei, Tobias Weinert, Przemyslaw Nogly, Petr Skopintsev, Ivan Usov, Filip Leonarski, Tian Geng, Mathieu Rappas, Andrew S. Doré, Robert Cooke, Shahrooz Nasrollahi Shirazi, Florian Dworkowski, May Sharpe, Natacha Olieric, Camila Bacellar, Rok Bohinc, Michel O. Steinmetz, Gebhard Schertler, Rafael Abela, Luc Patthey, Bernd Schmitt, Michael Hennig, Jörg Standfuss, Meitian Wang, Christopher J. Milne
Publikováno v:
IUCrJ, Vol 7, Iss 6, Pp 965-975 (2020)
Long-wavelength pulses from the Swiss X-ray free-electron laser (XFEL) have been used for de novo protein structure determination by native single-wavelength anomalous diffraction (native-SAD) phasing of serial femtosecond crystallography (SFX) data.
Externí odkaz:
https://doaj.org/article/ad7aad98478142d29b1d85fde6face15
Autor:
Karol Nass, Alexander Gorel, Malik M. Abdullah, Andrew V. Martin, Marco Kloos, Agostino Marinelli, Andrew Aquila, Thomas R. M. Barends, Franz-Josef Decker, R. Bruce Doak, Lutz Foucar, Elisabeth Hartmann, Mario Hilpert, Mark S. Hunter, Zoltan Jurek, Jason E. Koglin, Alexander Kozlov, Alberto A. Lutman, Gabriela Nass Kovacs, Christopher M. Roome, Robert L. Shoeman, Robin Santra, Harry M. Quiney, Beata Ziaja, Sébastien Boutet, Ilme Schlichting
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
The local X-ray-induced dynamics that occur in protein crystals during serial femtosecond crystallography (SFX) measurements at XFELs are not well understood. Here the authors performed a time-resolved X-ray pump X-ray probe SFX experiment, and they
Externí odkaz:
https://doaj.org/article/9afb811b5338411fb4f4557becfc7546
Autor:
Joyce Woodhouse, Gabriela Nass Kovacs, Nicolas Coquelle, Lucas M. Uriarte, Virgile Adam, Thomas R. M. Barends, Martin Byrdin, Eugenio de la Mora, R. Bruce Doak, Mikolaj Feliks, Martin Field, Franck Fieschi, Virginia Guillon, Stefan Jakobs, Yasumasa Joti, Pauline Macheboeuf, Koji Motomura, Karol Nass, Shigeki Owada, Christopher M. Roome, Cyril Ruckebusch, Giorgio Schirò, Robert L. Shoeman, Michel Thepaut, Tadashi Togashi, Kensuke Tono, Makina Yabashi, Marco Cammarata, Lutz Foucar, Dominique Bourgeois, Michel Sliwa, Jacques-Philippe Colletier, Ilme Schlichting, Martin Weik
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
rsEGFP2 is a reversibly photoswitchable fluorescent protein used in super-resolution light microscopy. Here the authors present the structure of an rsEGFP2 ground-state intermediate after excited state-decay that was obtained by nanosecond time-resol
Externí odkaz:
https://doaj.org/article/88972c410939421d85cfc000a74d2ee0
Autor:
Karol Nass, Lars Redecke, M. Perbandt, O. Yefanov, M. Klinge, R. Koopmann, F. Stellato, A. Gabdulkhakov, R. Schönherr, D. Rehders, J. M. Lahey-Rudolph, A. Aquila, A. Barty, S. Basu, R. B. Doak, R. Duden, M. Frank, R. Fromme, S. Kassemeyer, G. Katona, R. Kirian, H. Liu, I. Majoul, J. M. Martin-Garcia, M. Messerschmidt, R. L. Shoeman, U. Weierstall, S. Westenhoff, T. A. White, G. J. Williams, C. H. Yoon, N. Zatsepin, P. Fromme, M. Duszenko, H. N. Chapman, C. Betzel
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Trypanosoma brucei inosine-5′-monophosphate dehydrogenase (IMPDH) is an enzyme in the guanine nucleotide biosynthesis pathway and of interest as a drug target. Here the authors present the 2.8 Å room temperature structure of TbIMPDH determined by
Externí odkaz:
https://doaj.org/article/62386f11dbb14a64b2304040fafe13d2
Autor:
Cecilia M. Casadei, Karol Nass, Anton Barty, Mark S. Hunter, Celestino Padeste, Ching-Ju Tsai, Sébastien Boutet, Marc Messerschmidt, Leonardo Sala, Garth J. Williams, Dmitry Ozerov, Matthew Coleman, Xiao-Dan Li, Matthias Frank, Bill Pedrini
Publikováno v:
IUCrJ, Vol 6, Iss 1, Pp 34-45 (2019)
Serial femtosecond crystallography of two-dimensional membrane-protein crystals at X-ray free-electron lasers has the potential to address the dynamics of functionally relevant large-scale motions, which can be sterically hindered in three-dimensiona
Externí odkaz:
https://doaj.org/article/1a712444222c42ae9abe2b27756b4020