Simultaneous Femtosecond X-ray Spectroscopy and Diffraction of Photosystem II at Room Temperature

Author:

Kern Jan12,Alonso-Mori Roberto2,Tran Rosalie1,Hattne Johan1,Gildea Richard J.1,Echols Nathaniel1,Glöckner Carina3,Hellmich Julia3,Laksmono Hartawan4,Sierra Raymond G.4,Lassalle-Kaiser Benedikt1,Koroidov Sergey5,Lampe Alyssa1,Han Guangye1,Gul Sheraz1,DiFiore Dörte3,Milathianaki Despina2,Fry Alan R.2,Miahnahri Alan2,Schafer Donald W.2,Messerschmidt Marc2,Seibert M. Marvin2,Koglin Jason E.2,Sokaras Dimosthenis6,Weng Tsu-Chien6,Sellberg Jonas67,Latimer Matthew J.6,Grosse-Kunstleve Ralf W.1,Zwart Petrus H.1,White William E.2,Glatzel Pieter8,Adams Paul D.1,Bogan Michael J.24,Williams Garth J.2,Boutet Sébastien2,Messinger Johannes5,Zouni Athina3,Sauter Nicholas K.1,Yachandra Vittal K.1,Bergmann Uwe2,Yano Junko1

Affiliation:

1. Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

2. Linac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.

3. Max-Volmer-Laboratorium für Biophysikalische Chemie, Technische Universität, D-10623 Berlin, Germany.

4. PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.

5. Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, Umeå, Sweden.

6. Stanford Synchrotron Radiation Lightsource (SSRL), SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.

7. Department of Physics, AlbaNova, Stockholm University, S-106 91 Stockholm, Sweden.

8. European Synchrotron Radiation Facility, F-38043 Grenoble Cedex 9, France.

Abstract

One Protein, Two Probes A central challenge in the use of x-ray diffraction to characterize macromolecular structure is the propensity of the high-energy radiation to damage the sample during data collection. Recently, a powerful accelerator-based, ultrafast x-ray laser source has been used to determine the geometric structures of small protein crystals too fragile for conventional diffraction techniques. Kern et al. (p. 491 , published online 14 February) now pair this method with concurrent x-ray emission spectroscopy to probe electronic structure, as well as geometry, and were able to characterize the metal oxidation states in the oxygen-evolving complex within photosystem II crystals, while simultaneously verifying the surrounding protein structure.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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