Simultaneous Femtosecond X-ray Spectroscopy and Diffraction of Photosystem II at Room Temperature-Reference-Cited by-同舟云学术

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

Published:2013-04-26 Issue:6131 Volume:340 Page:491-495
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

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

Reference40 articles.

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2. A Synthetic Model of the Mn 3 Ca Subsite of the Oxygen-Evolving Complex in Photosystem II

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