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  • 1. Aquila, Andrew
    et al.
    Hunter, Mark S.
    Doak, R. Bruce
    Kirian, Richard A.
    Fromme, Petra
    White, Thomas A.
    Andreasson, Jakob
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Arnlund, David
    Bajt, Saša
    Barends, Thomas R. M.
    Barthelmess, Miriam
    Bogan, Michael J.
    Bostedt, Christoph
    Bottin, Hervé
    Bozek, John D.
    Caleman, Carl
    Coppola, Nicola
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    DePonte, Daniel P.
    Elser, Veit
    Epp, Sascha W.
    Erk, Benjamin
    Fleckenstein, Holger
    Foucar, Lutz
    Frank, Matthias
    Fromme, Raimund
    Graafsma, Heinz
    Grotjohann, Ingo
    Gumprecht, Lars
    Hajdu, Janos
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Hampton, Christina Y.
    Hartmann, Andreas
    Hartmann, Robert
    Hau-Riege, Stefan
    Hauser, Günter
    Hirsemann, Helmut
    Holl, Peter
    Holton, James M.
    Hömke, André
    Johansson, Linda
    Kimmel, Nils
    Kassemeyer, Stephan
    Krasniqi, Faton
    Kühnel, Kai-Uwe
    Liang, Mengning
    Lomb, Lukas
    Malmerberg, Erik
    Marchesini, Stefano
    Martin, Andrew V.
    Maia, Filipe R.N.C.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Messerschmidt, Marc
    Nass, Karol
    Reich, Christian
    Neutze, Richard
    Rolles, Daniel
    Rudek, Benedikt
    Rudenko, Artem
    Schlichting, Ilme
    Schmidt, Carlo
    Schmidt, Kevin E.
    Schulz, Joachim
    Seibert, M. Marvin
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Soltau, Heike
    Shoeman, Robert L.
    Sierra, Raymond
    Starodub, Dmitri
    Stellato, Francesco
    Stern, Stephan
    Strüder, Lothar
    Timneanu, Nicusor
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Ullrich, Joachim
    Wang, Xiaoyu
    Williams, Garth J.
    Weidenspointner, Georg
    Weierstall, Uwe
    Wunderer, Cornelia
    Barty, Anton
    Spence, John C. H.
    Chapman, Henry N.
    Time-resolved protein nanocrystallography using an X-ray free-electron laser2012In: Optics Express, ISSN 1094-4087, E-ISSN 1094-4087, Vol. 20, no 3, p. 2706-2716Article in journal (Refereed)
    Abstract [en]

    We demonstrate the use of an X-ray free electron laser synchronized with an optical pump laser to obtain X-ray diffraction snapshots from the photoactivated states of large membrane protein complexes in the form of nanocrystals flowing in a liquid jet. Light-induced changes of Photosystem I-Ferredoxin co-crystals were observed at time delays of 5 to 10 µs after excitation. The result correlates with the microsecond kinetics of electron transfer from Photosystem I to ferredoxin. The undocking process that follows the electron transfer leads to large rearrangements in the crystals that will terminally lead to the disintegration of the crystals. We describe the experimental setup and obtain the first time-resolved femtosecond serial X-ray crystallography results from an irreversible photo-chemical reaction at the Linac Coherent Light Source. This technique opens the door to time-resolved structural studies of reaction dynamics in biological systems.

  • 2. Arnlund, David
    et al.
    Johansson, Linda C
    Wickstrand, Cecilia
    Barty, Anton
    Williams, Garth J
    Malmerberg, Erik
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Milathianaki, Despina
    DePonte, Daniel P
    Shoeman, Robert L
    Wang, Dingjie
    James, Daniel
    Katona, Gergely
    Westenhoff, Sebastian
    White, Thomas A
    Aquila, Andrew
    Bari, Sadia
    Berntsen, Peter
    Bogan, Mike
    van Driel, Tim Brandt
    Doak, R Bruce
    Kjær, Kasper Skov
    Frank, Matthias
    Fromme, Raimund
    Grotjohann, Ingo
    Henning, Robert
    Hunter, Mark S
    Kirian, Richard A
    Kosheleva, Irina
    Kupitz, Christopher
    Liang, Mengning
    Martin, Andrew V
    Nielsen, Martin Meedom
    Messerschmidt, Marc
    Seibert, M Marvin
    Linac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, California, USA..
    Sjöhamn, Jennie
    Stellato, Francesco
    Weierstall, Uwe
    Zatsepin, Nadia A
    Spence, John C H
    Fromme, Petra
    Schlichting, Ilme
    Boutet, Sébastien
    Groenhof, Gerrit
    Chapman, Henry N
    Neutze, Richard
    Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser2014In: Nature Methods, ISSN 1548-7091, E-ISSN 1548-7105, Vol. 11, no 9, p. 923-926Article in journal (Refereed)
    Abstract [en]

    We describe a method to measure ultrafast protein structural changes using time-resolved wide-angle X-ray scattering at an X-ray free-electron laser. We demonstrated this approach using multiphoton excitation of the Blastochloris viridis photosynthetic reaction center, observing an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein. This provides direct structural evidence for a 'protein quake': the hypothesis that proteins rapidly dissipate energy through quake-like structural motions.

  • 3. Barty, Anton
    et al.
    Caleman, Carl
    Aquila, Andrew
    Timneanu, Nicusor
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Lomb, Lukas
    White, Thomas A.
    Andreasson, Jakob
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Arnlund, David
    Bajt, Sasa
    Barends, Thomas R. M.
    Barthelmess, Miriam
    Bogan, Michael J.
    Bostedt, Christoph
    Bozek, John D.
    Coffee, Ryan
    Coppola, Nicola
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    DePonte, Daniel P.
    Doak, R. Bruce
    Ekeberg, Tomas
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Elser, Veit
    Epp, Sascha W.
    Erk, Benjamin
    Fleckenstein, Holger
    Foucar, Lutz
    Fromme, Petra
    Graafsma, Heinz
    Gumprecht, Lars
    Hajdu, Janos
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Hampton, Christina Y.
    Hartmann, Robert
    Hartmann, Andreas
    Hauser, Guenter
    Hirsemann, Helmut
    Holl, Peter
    Hunter, Mark S.
    Johansson, Linda
    Kassemeyer, Stephan
    Kimmel, Nils
    Kirian, Richard A.
    Liang, Mengning
    Maia, Filipe R. N. C.
    Malmerberg, Erik
    Marchesini, Stefano
    Martin, Andrew V.
    Nass, Karol
    Neutze, Richard
    Reich, Christian
    Rolles, Daniel
    Rudek, Benedikt
    Rudenko, Artem
    Scott, Howard
    Schlichting, Ilme
    Schulz, Joachim
    Seibert, M. Marvin
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Shoeman, Robert L.
    Sierra, Raymond G.
    Soltau, Heike
    Spence, John C. H.
    Stellato, Francesco
    Stern, Stephan
    Strueder, Lothar
    Ullrich, Joachim
    Wang, X.
    Weidenspointner, Georg
    Weierstall, Uwe
    Wunderer, Cornelia B.
    Chapman, Henry N.
    Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements2012In: Nature Photonics, ISSN 1749-4885, E-ISSN 1749-4893, Vol. 6, no 1, p. 35-40Article in journal (Refereed)
    Abstract [en]

    X-ray free-electron lasers have enabled new approaches to the structural determination of protein crystals that are too small or radiation-sensitive for conventional analysis(1). For sufficiently short pulses, diffraction is collected before significant changes occur to the sample, and it has been predicted that pulses as short as 10 fs may be required to acquire atomic-resolution structural information(1-4). Here, we describe a mechanism unique to ultrafast, ultra-intense X-ray experiments that allows structural information to be collected from crystalline samples using high radiation doses without the requirement for the pulse to terminate before the onset of sample damage. Instead, the diffracted X-rays are gated by a rapid loss of crystalline periodicity, producing apparent pulse lengths significantly shorter than the duration of the incident pulse. The shortest apparent pulse lengths occur at the highest resolution, and our measurements indicate that current X-ray free-electron laser technology(5) should enable structural determination from submicrometre protein crystals with atomic resolution.

  • 4.
    Borg, O. Anders
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Quantum Chemistry.
    Karlsson, Daniel
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Photochemistry and Molecular Science.
    Isomäki-Krondahl, Magnus
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Quantum Chemistry.
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Photochemistry and Molecular Science.
    Lunell, Sten
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Quantum Chemistry.
    Predissociation of Chlorobenzene, beyond the pseudo-diatomic model2008In: Chemical Physics Letters, ISSN 0009-2614, E-ISSN 1873-4448, Vol. 456, no 4-6, p. 123-126Article in journal (Refereed)
    Abstract [en]

    Dissociation of chlorobenzene via the lowest singlet excited state has been investigated by means of pump-probe femtosecond spectroscopy and spin-orbit corrected ab initio quantum chemistry. We have found that the so far accepted model with a (1)pi pi* -> (3)pi/n sigma* reaction mechanism has to be amended. We suggest that the mechanism goes via a transition from (1)pi pi* to a pi sigma* state that is to 90% a singlet. Further, three nuclear degrees of freedom required to describe the dissociation have been defined.

  • 5.
    Borg, O Anders
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Physics, Department of Quantum Chemistry. Chemistry, Department of Physical and Analytical Chemistry, Quantum Chemistry. Department of Physics and Materials Science, Chemical Physics. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry. Avdelningen för kvantkemi.
    Liu, Ya-Jun
    Persson, Petter
    Lunell, Sten
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Physics, Department of Quantum Chemistry. Chemistry, Department of Physical and Analytical Chemistry, Quantum Chemistry. Department of Physics and Materials Science, Chemical Physics. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry. Avdelningen för kvantkemi.
    Karlsson, Daniel
    Department of Photochemistry and Molecular Science. Chemistry, Department of Physical and Analytical Chemistry, Quantum Chemistry. Department of Physics and Materials Science, Chemical Physics.
    Kadi, Malin
    Davidsson, Jan
    Department of Photochemistry and Molecular Science. Chemistry, Department of Physical and Analytical Chemistry, Quantum Chemistry. Department of Physics and Materials Science, Chemical Physics.
    Photochemistry of bromofluorobenzenes.2006In: J Phys Chem A Mol Spectrosc Kinet Environ Gen Theory, ISSN 1089-5639, Vol. 110, no 22, p. 7045-56Article in journal (Refereed)
  • 6.
    Davidsson, Jan
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry. Department of Physical and Analytical Chemistry, Physical Chemistry I.
    Poulsen, Jens
    Cammarata, Marco
    Georgiou, Panayiotis
    Wouts, Remco
    Katona, Gergely
    Jacobson, Frida
    Plech, Anton
    Wulff, Michael
    Nyman, Gunnar
    Neutze, Richard
    Structural Determination of a Transient Isomer of CH2I2 by Picosecond X-Ray Diffraction.2005In: Phys Rev Lett, ISSN 0031-9007, Vol. 94, no 24, p. 245503-Article in journal (Refereed)
  • 7.
    Dods, Robert
    et al.
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Båth, Petra
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Arnlund, David
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Beyerlein, Kenneth R.
    Deutsch Elektronen Synchrotron DESY, Ctr Free Electron Laser Sci, Hamburg, Germany..
    Nelson, Garrett
    Arizona State Univ, Dept Phys, Tempe, AZ 85287 USA..
    Liang, Mengling
    Stanford Linear Accelerator Ctr SLAC Natl Acceler, Linac Coherent Light Source, Menlo Pk, CA USA..
    Harimoorthy, Rajiv
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Berntsen, Peter
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden.;La Trobe Univ, Australian Res Council Ctr Excellence Adv Mol Ima, La Trobe Inst Mol Sci, Bundoora, Vic 3086, Australia..
    Malmerberg, Erik
    Lawrence Berkeley Natl Lab, Phys Biosci Div, 1 Cyclotron Rd, Berkeley, CA 94720 USA..
    Johansson, Linda
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden.;Univ Southern Calif, Bridge Inst, Dept Chem, Los Angeles, CA 90089 USA..
    Andersson, Rebecka
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Bosman, Robert
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Carbajo, Sergio
    Stanford Linear Accelerator Ctr SLAC Natl Acceler, Linac Coherent Light Source, Menlo Pk, CA USA..
    Claesson, Elin
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Conrad, Chelsie E.
    Arizona State Univ, Dept Phys, Tempe, AZ 85287 USA..
    Dahl, Peter
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Hammarin, Greger
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Hunter, Mark S.
    Stanford Linear Accelerator Ctr SLAC Natl Acceler, Linac Coherent Light Source, Menlo Pk, CA USA..
    Li, Chufeng
    Arizona State Univ, Dept Phys, Tempe, AZ 85287 USA..
    Lisova, Stella
    Arizona State Univ, Dept Phys, Tempe, AZ 85287 USA..
    Milathianaki, Despina
    Stanford Linear Accelerator Ctr SLAC Natl Acceler, Linac Coherent Light Source, Menlo Pk, CA USA..
    Robinson, Joseph
    Stanford Linear Accelerator Ctr SLAC Natl Acceler, Linac Coherent Light Source, Menlo Pk, CA USA..
    Safari, Cecilia
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Sharma, Amit
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Williams, Garth
    Stanford Linear Accelerator Ctr SLAC Natl Acceler, Linac Coherent Light Source, Menlo Pk, CA USA..
    Wickstrand, Cecilia
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Yefanov, Oleksandr
    Deutsch Elektronen Synchrotron DESY, Ctr Free Electron Laser Sci, Hamburg, Germany..
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    DePonte, Daniel P.
    Deutsch Elektronen Synchrotron DESY, Ctr Free Electron Laser Sci, Hamburg, Germany..
    Barty, Anton
    Deutsch Elektronen Synchrotron DESY, Ctr Free Electron Laser Sci, Hamburg, Germany..
    Branden, Gisela
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    Neutze, Richard
    Univ Gothenburg, Dept Chem & Mol Biol, Gothenburg, Sweden..
    From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography2017In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 25, no 9, p. 1461-1468Article in journal (Refereed)
    Abstract [en]

    Serial protein crystallography was developed at X-ray free-electron lasers (XFELs) and is now also being applied at storage ring facilities. Robust strategies for the growth and optimization of microcrystals are needed to advance the field. Here we illustrate a generic strategy for recovering high-density homogeneous samples of microcrystals starting from conditions known to yield large (macro) crystals of the photosynthetic reaction center of Blastochloris viridis (RCvir). We first crushed these crystals prior to multiple rounds of microseeding. Each cycle of microseeding facilitated improvements in the RCvir serial femtosecond crystallography (SFX) structure from 3.3-angstrom to 2.4-angstrom resolution. This approach may allow known crystallization conditions for other proteins to be adapted to exploit novel scientific opportunities created by serial crystallography.

  • 8. Georgiou, Panayiotis
    et al.
    Vincent, Jonathan
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Photochemistry and Molecular Science. Physics, Department of Physics and Materials Science, Chemical Physics.
    Andersson, Magnus
    Wohri, Annemarie B
    Gourdon, Pontus
    Poulsen, Jens
    Davidsson, Jan
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Photochemistry and Molecular Science. Physics, Department of Physics and Materials Science, Chemical Physics.
    Neutze, Richard
    Picosecond calorimetry: time-resolved x-ray diffraction studies of liquid CH2Cl2.2006In: J Chem Phys, ISSN 0021-9606, Vol. 124, no 23, p. 234507-Article in journal (Refereed)
  • 9. Johansson, Linda C.
    et al.
    Arnlund, David
    Katona, Gergely
    White, Thomas A.
    Barty, Anton
    DePonte, Daniel P.
    Shoeman, Robert L.
    Wickstrand, Cecilia
    Sharma, Amit
    Williams, Garth J.
    Aquila, Andrew
    Bogan, Michael J.
    Caleman, Carl
    Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany.
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Doak, R. Bruce
    Frank, Matthias
    Fromme, Raimund
    Galli, Lorenzo
    Grotjohann, Ingo
    Hunter, Mark S.
    Kassemeyer, Stephan
    Kirian, Richard A.
    Kupitz, Christopher
    Liang, Mengning
    Lomb, Lukas
    Malmerberg, Erik
    Martin, Andrew V.
    Messerschmidt, Marc
    Nass, Karol
    Redecke, Lars
    Seibert, M. Marvin
    Linac Coherent Light Source, LCLS, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, 94025 California, USA.
    Sjoehamn, Jennie
    Steinbrener, Jan
    Stellato, Francesco
    Wang, Dingjie
    Wahlgren, Weixaio Y.
    Weierstall, Uwe
    Westenhoff, Sebastian
    Zatsepin, Nadia A.
    Boutet, Sebastien
    Spence, John C. H.
    Schlichting, Ilme
    Chapman, Henry N.
    Fromme, Petra
    Neutze, Richard
    Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography2013In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 4, no Article nr:2911Article in journal (Refereed)
    Abstract [en]

    Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 angstrom resolution and determine its serial femtosecond crystallography structure to 3.5 angstrom resolution. Although every microcrystal is exposed to a dose of 33MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.

  • 10. Johansson, Linda C
    et al.
    Arnlund, David
    White, Thomas A
    Katona, Gergely
    DePonte, Daniel P
    Weierstall, Uwe
    Doak, R Bruce
    Shoeman, Robert L
    Lomb, Lukas
    Malmerberg, Erik
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Nass, Karol
    Liang, Mengning
    Andreasson, Jakob
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Aquila, Andrew
    Bajt, Sasa
    Barthelmess, Miriam
    Barty, Anton
    Bogan, Michael J
    Bostedt, Christoph
    Bozek, John D
    Caleman, Carl
    Coffee, Ryan
    Coppola, Nicola
    Ekeberg, Tomas
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Epp, Sascha W
    Erk, Benjamin
    Fleckenstein, Holger
    Foucar, Lutz
    Graafsma, Heinz
    Gumprecht, Lars
    Hajdu, Janos
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Hampton, Christina Y
    Hartmann, Robert
    Hartmann, Andreas
    Hauser, Gunter
    Hirsemann, Helmut
    Holl, Peter
    Hunter, Mark S
    Kassemeyer, Stephan
    Kimmel, Nils
    Kirian, Richard A
    Maia, Filipe R N C
    Marchesini, Stefano
    Martin, Andrew V
    Reich, Christian
    Rolles, Daniel
    Rudek, Benedikt
    Rudenko, Artem
    Schlichting, Ilme
    Schulz, Joachim
    Seibert, M Marvin
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Sierra, Raymond G
    Soltau, Heike
    Starodub, Dmitri
    Stellato, Francesco
    Stern, Stephan
    Struder, Lothar
    Timneanu, Nicusor
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
    Ullrich, Joachim
    Wahlgren, Weixiao Y
    Wang, Xiaoyu
    Weidenspointner, Georg
    Wunderer, Cornelia
    Fromme, Petra
    Chapman, Henry N
    Spence, John C H
    Neutze, Richard
    Lipidic phase membrane protein serial femtosecond crystallography2012In: Nature Methods, ISSN 1548-7091, E-ISSN 1548-7105, Vol. 9, no 3, p. 263-265Article in journal (Refereed)
    Abstract [en]

    X-ray free electron laser (X-FEL)-based serial femtosecond crystallography is an emerging method with potential to rapidly advance the challenging field of membrane protein structural biology. Here we recorded interpretable diffraction data from micrometer-sized lipidic sponge phase crystals of the Blastochloris viridis photosynthetic reaction center delivered into an X-FEL beam using a sponge phase micro-jet.

  • 11.
    Kubo, Minoru
    et al.
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Japan Sci & Technol Agcy, PRESTO, 4-1-8 Honcho, Kawaguchi, Saitama 3320012, Japan..
    Nango, Eriko
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Kyoto Univ, Grad Sch Med, Dept Cell Biol, Sakyo Ku, Yoshidakonoe Cho, Kyoto 6068501, Japan..
    Tono, Kensuke
    Japan Synchrotron Radiat Res Inst, 1-1-1 Kouto, Sayo, Hyogo 6795198, Japan..
    Kimura, Tetsunari
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Kobe Univ, Grad Sch Sci, Dept Chem, Nada Ku, 1-1 Rokkodai, Kobe, Hyogo 6578501, Japan..
    Owada, Shigeki
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Song, Changyong
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Pohang Univ Sci & Technol, Dept Phys, Pohang 790784, South Korea..
    Mafune, Fumitaka
    Univ Tokyo, Sch Arts & Sci, Dept Basic Sci, Meguro Ku, Tokyo 1538902, Japan..
    Miyajima, Ken
    Univ Tokyo, Sch Arts & Sci, Dept Basic Sci, Meguro Ku, Tokyo 1538902, Japan..
    Takeda, Yoshihiro
    Genesis Res Inst Inc, East Tokyo Lab, Ichikawa, Chiba 2720001, Japan..
    Kohno, Jun-ya
    Gakushuin Univ, Sch Sci, Dept Chem, Toshima Ku, Tokyo, Japan..
    Miyauchi, Naoya
    Natl Inst Mat Sci, Res Ctr Adv Measurement & Characterizat, Tsukuba, Ibaraki 3050047, Japan..
    Nakane, Takanori
    Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Bunkyo Ku, 7-3-1 Hongo, Tokyo 1130033, Japan..
    Tanaka, Tomoyuki
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Nomura, Takashi
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Tanaka, Rie
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Murata, Michio
    Osaka Univ, Lipid Act Struct Project, JST ERATO, 1-1 Machikaneyama, Toyonaka, Osaka 5600043, Japan..
    Kameshima, Takashi
    Japan Synchrotron Radiat Res Inst, 1-1-1 Kouto, Sayo, Hyogo 6795198, Japan..
    Hatsui, Takaki
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Joti, Yasumasa
    Japan Synchrotron Radiat Res Inst, 1-1-1 Kouto, Sayo, Hyogo 6795198, Japan..
    Neutze, Richard
    Univ Gothenburg, Dept Chem & Mol Biol, Box 462, SE-40530 Gothenburg, Sweden..
    Yabashi, Makina
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Iwata, So
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Kyoto Univ, Grad Sch Med, Dept Cell Biol, Sakyo Ku, Yoshidakonoe Cho, Kyoto 6068501, Japan..
    Nanosecond pump-probe device for time-resolved serial femtosecond crystallography developed at SACLA2017In: Journal of Synchrotron Radiation, ISSN 0909-0495, E-ISSN 1600-5775, Vol. 24, p. 1086-1091Article in journal (Refereed)
    Abstract [en]

    X-ray free-electron lasers (XFELs) have opened new opportunities for timeresolved X-ray crystallography. Here a nanosecond optical-pump XFEL-probe device developed for time-resolved serial femtosecond crystallography (TRSFX) studies of photo-induced reactions in proteins at the SPring-8 Angstrom Compact free-electron LAser (SACLA) is reported. The optical-fiber-based system is a good choice for a quick setup in a limited beam time and allows pump illumination from two directions to achieve high excitation efficiency of protein microcrystals. Two types of injectors are used: one for extruding highly viscous samples such as lipidic cubic phase (LCP) and the other for pulsed liquid droplets. Under standard sample flow conditions from the viscous-sample injector, delay times from nanoseconds to tens of milliseconds are accessible, typical time scales required to study large protein conformational changes. A first demonstration of a TR-SFX experiment on bacteriorhodopsin in bicelle using a setup with a droplet-type injector is also presented.

  • 12.
    Marcellini, Moreno
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Computational Biology and Bioinformatics. CNRS St Gobain, UMR3080, Ceram Synth & Functionalizat Lab, F-84306 Cavaillon, France.;Univ Bourgogne Franche Comte, Inst UTINAM, UMR 6213, CNRS, 16 Route Gray, F-25030 Besancon, France..
    Nasedkin, Alexandr
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry. Chalmers Univ Technol, Dept Phys, SE-41296 Gothenburg, Sweden..
    Zietz, Burkhard
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Petersson, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Vincent, Jonathan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Palazzetti, Federico
    Univ Perugia, Dipartimento Chim Biol & Biotecnol, I-06123 Perugia, Italy..
    Malmerberg, Erik
    Univ Gothenburg, Dept Chem & Mol Biol, SE-40530 Gothenburg, Sweden.;AstraZeneca, Pepparedsleden 1, SE-43150 Gothenburg, Sweden..
    Kong, Qingyu
    Argonne Natl Labs, Xray Sci Div, 9700 S Cass Ave, Argonne, IL 60439 USA.;European Synchrotron Radiat Facil, BP 220, F-38043 Grenoble, France..
    Wulff, Michael
    European Synchrotron Radiat Facil, BP 220, F-38043 Grenoble, France..
    van der Spoel, David
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Computational Biology and Bioinformatics.
    Neutze, Richard
    Univ Gothenburg, Dept Chem & Mol Biol, SE-40530 Gothenburg, Sweden..
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Transient isomers in the photodissociation of bromoiodomethane2018In: Journal of Chemical Physics, ISSN 0021-9606, E-ISSN 1089-7690, Vol. 148, no 13, article id 134307Article in journal (Refereed)
    Abstract [en]

    The photochemistry of halomethanes is fascinating for the complex cascade reactions toward either the parent or newly synthesized molecules. Here, we address the structural rearrangement of photodissociated CH2IBr in methanol and cyclohexane, probed by time-resolved X-ray scattering in liquid solution. Upon selective laser cleavage of the C-I bond, we follow the reaction cascade of the two geminate geometrical isomers, CH2I-Br and CH2Br-I. Both meta-stable isomers decay on different time scales, mediated by solvent interaction, toward the original parent molecule. We observe the internal rearrangement of CH2Br-I to CH2I-Br in cyclohexane by extending the time window up to 3 mu s. We track the photoproduct kinetics of CH2Br-I in methanol solution where only one isomer is observed. The effect of the polarity of solvent on the geminate recombination pathways is discussed.

  • 13.
    Nango, Eriko
    et al.
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Kyoto Univ, Dept Cell Biol, Grad Sch Med, Sakyo Ku, Yoshidakonoe Cho, Kyoto 6068501, Japan..
    Royant, Antoine
    Univ Grenoble Alpes, CNRS, Commissariat Energie Atom & Energies Alternat, Inst Biol Struct, F-38044 Grenoble, France.;European Synchrotron Radiat Facil, F-38043 Grenoble, France..
    Kubo, Minoru
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Japan Sci & Technol Agcy JST, Precursory Res Embryon Sci & Technol PRESTO, 4-1-8 Honcho, Kawaguchi, Saitama 3320012, Japan..
    Nakane, Takanori
    Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Bunkyo Ku, 2-11-16 Yayoi, Tokyo 1130032, Japan..
    Wickstrand, Cecilia
    Univ Gothenburg, Dept Chem & Mol Biol, Box 462, SE-40530 Gothenburg, Sweden..
    Kimura, Tetsunari
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Kobe Univ, Grad Sch Sci, Dept Chem, Nada Ku, 1-1 Rokkodai, Kobe, Hyogo 6578501, Japan..
    Tanaka, Tomoyuki
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Tono, Kensuke
    Japan Synchrotron Radiat Res Inst, 1-1-1 Kouto, Sayo, Hyogo 6795198, Japan..
    Song, Changyong
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Pohang Univ Sci & Technol, Dept Phys, Pohang 790784, South Korea..
    Tanaka, Rie
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Arima, Toshi
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Yamashita, Ayumi
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Kobayashi, Jun
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Hosaka, Toshiaki
    RIKEN Ctr Life Sci Technol, Div Struct & Synthet Biol, Tsurumi Ku, 1-7-22 Suehiro Cho, Yokohama, Kanagawa 2300045, Japan..
    Mizohata, Eiichi
    Osaka Univ, Grad Sch Engn, Dept Appl Chem, 2-1 Yamadaoka, Suita, Osaka 5650871, Japan..
    Nogly, Przemyslaw
    Paul Scherrer Inst, Lab Biomol Res, Div Biol & Chem, CH-5232 Villigen, Switzerland..
    Sugahara, Michihiro
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Nam, Daewoong
    Pohang Univ Sci & Technol, Dept Phys, Pohang 790784, South Korea..
    Nomura, Takashi
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Shimamura, Tatsuro
    Kyoto Univ, Dept Cell Biol, Grad Sch Med, Sakyo Ku, Yoshidakonoe Cho, Kyoto 6068501, Japan..
    Im, Dohyun
    Kyoto Univ, Dept Cell Biol, Grad Sch Med, Sakyo Ku, Yoshidakonoe Cho, Kyoto 6068501, Japan..
    Fujiwara, Takaaki
    Kyoto Univ, Dept Cell Biol, Grad Sch Med, Sakyo Ku, Yoshidakonoe Cho, Kyoto 6068501, Japan..
    Yamanaka, Yasuaki
    Kyoto Univ, Dept Cell Biol, Grad Sch Med, Sakyo Ku, Yoshidakonoe Cho, Kyoto 6068501, Japan..
    Jeon, Byeonghyun
    Pohang Univ Sci & Technol, Dept Phys, Pohang 790784, South Korea..
    Nishizawa, Tomohiro
    Japan Sci & Technol Agcy JST, Precursory Res Embryon Sci & Technol PRESTO, 4-1-8 Honcho, Kawaguchi, Saitama 3320012, Japan.;Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Bunkyo Ku, 2-11-16 Yayoi, Tokyo 1130032, Japan..
    Oda, Kazumasa
    Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Bunkyo Ku, 2-11-16 Yayoi, Tokyo 1130032, Japan..
    Fukuda, Masahiro
    Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Bunkyo Ku, 2-11-16 Yayoi, Tokyo 1130032, Japan..
    Andersson, Rebecka
    Univ Gothenburg, Dept Chem & Mol Biol, Box 462, SE-40530 Gothenburg, Sweden..
    Bath, Petra
    Univ Gothenburg, Dept Chem & Mol Biol, Box 462, SE-40530 Gothenburg, Sweden..
    Dods, Robert
    Univ Gothenburg, Dept Chem & Mol Biol, Box 462, SE-40530 Gothenburg, Sweden..
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Matsuoka, Shigeru
    Osaka Univ, Lipid Act Struct Project, JST Exploratory Res Adv Technol ERATO, 1-1 Machikaneyama, Toyonaka, Osaka 5600043, Japan..
    Kawatake, Satoshi
    Osaka Univ, Lipid Act Struct Project, JST Exploratory Res Adv Technol ERATO, 1-1 Machikaneyama, Toyonaka, Osaka 5600043, Japan..
    Murata, Michio
    Osaka Univ, Lipid Act Struct Project, JST Exploratory Res Adv Technol ERATO, 1-1 Machikaneyama, Toyonaka, Osaka 5600043, Japan..
    Nureki, Osamu
    Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Bunkyo Ku, 2-11-16 Yayoi, Tokyo 1130032, Japan..
    Owada, Shigeki
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Kameshima, Takashi
    Japan Synchrotron Radiat Res Inst, 1-1-1 Kouto, Sayo, Hyogo 6795198, Japan..
    Hatsui, Takaki
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Joti, Yasumasa
    Japan Synchrotron Radiat Res Inst, 1-1-1 Kouto, Sayo, Hyogo 6795198, Japan..
    Schertler, Gebhard
    Paul Scherrer Inst, Lab Biomol Res, Div Biol & Chem, CH-5232 Villigen, Switzerland.;Swiss Fed Inst Technol, Dept Biol, CH-8093 Zurich, Switzerland..
    Yabashi, Makina
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan..
    Bondar, Ana-Nicoleta
    Free Univ Berlin, Dept Phys, Theoret Mol Biophys, Arnimallee 14, D-14195 Berlin, Germany..
    Standfuss, Jorg
    Paul Scherrer Inst, Lab Biomol Res, Div Biol & Chem, CH-5232 Villigen, Switzerland..
    Neutze, Richard
    Univ Gothenburg, Dept Chem & Mol Biol, Box 462, SE-40530 Gothenburg, Sweden..
    Iwata, So
    RIKEN SPring 8 Ctr, 1-1-1 Kouto, Sayo, Hyogo 6795148, Japan.;Kyoto Univ, Dept Cell Biol, Grad Sch Med, Sakyo Ku, Yoshidakonoe Cho, Kyoto 6068501, Japan..
    A three-dimensional movie of structural changes in bacteriorhodopsin2016In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 354, no 6319, p. 1552-1557Article in journal (Refereed)
    Abstract [en]

    Bacteriorhodopsin (bR) is a light-driven proton pump and a model membrane transport protein. We used time-resolved serial femtosecond crystallography at an x-ray free electron laser to visualize conformational changes in bR from nanoseconds to milliseconds following photoactivation. An initially twisted retinal chromophore displaces a conserved tryptophan residue of transmembrane helix F on the cytoplasmic side of the protein while dislodging a key water molecule on the extracellular side. The resulting cascade of structural changes throughout the protein shows how motions are choreographed as bR transports protons uphill against a transmembrane concentration gradient.

  • 14.
    Nasedkin, Alexandr
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Kumpugdee-Vollrath, Mont
    Determination of nanostructure of liposomes containing two model drugs by X-ray scattering from a synchrotron source2013In: Journal of Synchrotron Radiation, ISSN 0909-0495, E-ISSN 1600-5775, Vol. 20, p. 721-728Article in journal (Refereed)
    Abstract [en]

    Small-angle X-ray scattering has been employed to study how the introduction of paracetamol and acetylsalicylic acid into a liposome bilayer system affects the system's nanostructure. An X-ray scattering model, developed for multilamellar liposome systems [Pabst et al. (2000), Phys. Rev. E, 62, 4000-4009], has been used to fit the experimental data and to extract information on how structural parameters, such as the number and thickness of the bilayers of the liposomes, thickness of the water layer in between the bilayers, size and volume of the head and tail groups, are affected by the drugs and their concentration. Even though the experimental data reveal a complicated picture of the drug-bilayer interaction, they clearly show a correlation between nanostructure, drug and concentration in some aspects. The localization of the drugs in the bilayers is discussed.

  • 15.
    Nasedkin, Alexandr
    et al.
    Chalmers Univ Technol, Dept Phys, Gothenburg.
    Davidsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
    Niemi, Antti J.
    Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Theoretical Physics. Chalmers Univ Technol, Dept Phys, Gothenburg; Stockholm Univ, NORDITA, Stockholm; Univ Tours, Federat Denis Poisson, CNRS UMR 6083, Lab Math & Phys Theor, Parc Grandmont, Tours; Beijing Inst Technol, Sch Phys, Beijing; Far Eastern Fed Univ, Sch Biomed, Lab Phys Living Matter, Vladivostok.
    Peng, Xubiao
    Univ British Columbia, Dept Phys & Astron, Vancouver.
    Solution x-ray scattering and structure formation in protein dynamics2017In: Physical review. E, ISSN 2470-0045, E-ISSN 2470-0053, Vol. 96, no 6, article id 062405Article in journal (Refereed)
    Abstract [en]

    We propose a computationally effective approach that builds on Landau mean-field theory in combination with modern nonequilibrium statistical mechanics to model and interpret protein dynamics and structure formation in small- to wide-angle x-ray scattering (S/WAXS) experiments. We develop the methodology by analyzing experimental data in the case of Engrailed homeodomain protein as an example. We demonstrate how to interpret S/WAXS data qualitatively with a good precision and over an extended temperature range. We explain experimental observations in terms of protein phase structure, and we make predictions for future experiments and for how to analyze data at different ambient temperature values. We conclude that the approach we propose has the potential to become a highly accurate, computationally effective, and predictive tool for analyzing S/WAXS data. For this, we compare our results with those obtained previously in an all-atom molecular dynamics simulation.

  • 16. Odelius, Michael
    et al.
    Kadi, Malin
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry. Department of Physical and Analytical Chemistry, Physical Chemistry I.
    Davidsson, Jan
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry. Department of Physical and Analytical Chemistry, Physical Chemistry I.
    Tarnovsky, Alexander
    Photodissociation of diiodomethane in acetonitrile solution and fragment recombination into iso-diiodomethane studied with ab initio molecular dynamics simulations2004In: Journal of Chemical Physics, Vol. 121, no 5, p. 2208-2214Article in journal (Refereed)
  • 17.
    Wallin, Staffan
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry. Department of Biochemistry and Organic Chemistry, Organic Chemistry I. Department of Physical and Analytical Chemistry, Physical Chemistry I. Physics, Department of Physics and Materials Science, Chemical Physics.
    Davidsson, Jan
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry. Department of Biochemistry and Organic Chemistry, Organic Chemistry I. Department of Physical and Analytical Chemistry, Physical Chemistry I. Physics, Department of Physics and Materials Science, Chemical Physics.
    Modin, Judit
    Department of Chemistry. Department of Biochemistry and Organic Chemistry, Organic Chemistry I. Department of Physical and Analytical Chemistry, Physical Chemistry I. Physics, Department of Physics and Materials Science, Chemical Physics. Organisk kemi.
    Hammarström, Leif
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry. Department of Biochemistry and Organic Chemistry, Organic Chemistry I. Department of Physical and Analytical Chemistry, Physical Chemistry I. Physics, Department of Physics and Materials Science, Chemical Physics.
    Femtosecond Transient Absorption Anisotropy Study on [Ru(bpy)3]2+ and [Ru(bpy)(py)4]2+. Ultrafast Interligand Randomization of the MLCT State2005In: J. Phys. Chem. A, no 109, p. 4697-4704Article in journal (Refereed)
    Abstract [en]

    It is known that the relaxed excited state of [Ru(bpy)3]2+ is best described as a metal to ligand charge transfer (MLCT) state having one formally reduced bipyridine and two neutral. Previous reports have suggested [Malone, R. et al. J.Chem. Phys 1991, 95, 8970] that the electron "hops" from ligand to ligand in the MLCT state with a time constant of about 50 ps in acetonitrile. However, we have done transient absorption anisotropy measurements indicating that already after one picosecond the molecule has no memory of which bipyridine was initially photoselected, which suggest an ultrafast interligand randomization of the MLCT state.

1 - 17 of 17
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