S
Sébastien Boutet
Researcher at SLAC National Accelerator Laboratory
Publications - 221
Citations - 19765
Sébastien Boutet is an academic researcher from SLAC National Accelerator Laboratory. The author has contributed to research in topics: Femtosecond & Laser. The author has an hindex of 61, co-authored 207 publications receiving 17171 citations. Previous affiliations of Sébastien Boutet include Lawrence Livermore National Laboratory & Fermilab.
Papers
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Journal ArticleDOI
High-accuracy wavefront sensing for x-ray free electron lasers
Yanwei Liu,Matthew Seaberg,Diling Zhu,Jacek Krzywinski,Frank Seiboth,Corey L. Hardin,Daniele Cocco,Andrew Aquila,Bob Nagler,Hae Ja Lee,Sébastien Boutet,Yiping Feng,Yuantao Ding,Gabriel Marcus,Anne Sakdinawat +14 more
TL;DR: In this paper, a single-shot wavefront sensor for x-ray free electron laser (FEL) beams using single grating Talbot interferometry has been developed, which can be used to systematically study the wavefront from the FEL output, beam transport optics, and endstation focusing optics.
Journal ArticleDOI
Stimulated X-Ray Emission Spectroscopy in Transition Metal Complexes
Thomas Kroll,Clemens Weninger,Clemens Weninger,Roberto Alonso-Mori,Dimosthenis Sokaras,Diling Zhu,Laurent Mercadier,Vinay P. Majety,Agostino Marinelli,Alberto Lutman,Marc W. Guetg,Franz-Josef Decker,Sébastien Boutet,Andrew Aquila,Jason E. Koglin,Jake Koralek,Daniel P. DePonte,Jan Kern,Jan Kern,Franklin D. Fuller,Ernest Pastor,Thomas Fransson,Yu Zhang,Junko Yano,Vittal K. Yachandra,Nina Rohringer,Nina Rohringer,Uwe Bergmann +27 more
TL;DR: The observation and analysis of the gain curve of amplified Kα x-ray emission from solutions of Mn(II) and Mn(VII) complexes using an x-rays free electron laser to create the 1s core-hole population inversion is reported.
Journal ArticleDOI
Sacrificial tamper slows down sample explosion in FLASH diffraction experiments.
Stefan P. Hau-Riege,Sébastien Boutet,Anton Barty,Saša Bajt,Michael J. Bogan,Matthias Frank,Jakob Andreasson,Bianca Iwan,M. Marvin Seibert,Janos Hajdu,Anne Sakdinawat,Joachim Schulz,Rolf Treusch,Henry N. Chapman +13 more
TL;DR: It is shown that the lifetime of a nanostructured sample can be extended to several picoseconds by a tamper layer to dampen and quench the sample explosion, making <1 nm resolution imaging feasible.
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Structural dynamics in proteins induced by and probed with X-ray free-electron laser pulses.
Karol Nass,A. Gorel,Malik Muhammad Abdullah,Andrew V. Martin,Marco Kloos,Agostino Marinelli,Andrew Aquila,Thomas R. M. Barends,Franz-Josef Decker,R. Bruce Doak,Lutz Foucar,Elisabeth Hartmann,M. Hilpert,Mark S. Hunter,Zoltan Jurek,Jason E. Koglin,Alexander Kozlov,Alberto Lutman,Gabriela Nass Kovacs,C.M. Roome,Robert L. Shoeman,Robin Santra,Harry M. Quiney,B. Ziaja,B. Ziaja,Sébastien Boutet,Ilme Schlichting +26 more
TL;DR: A femtosecond time-resolved X-ray pump/X-ray probe SFX experiment on protein nanocrystals observes distinct structural changes in the disulfide bridges and peptide backbone of proteins; complementing theoretical approaches allow them to further characterize the details of the X- Ray induced ionization and local structural dynamics.
Journal ArticleDOI
X-ray laser diffraction for structure determination of the rhodopsin-arrestin complex.
X. Edward Zhou,Xiang Gao,Anton Barty,Yanyong Kang,Yuanzheng He,Wei Liu,Andrii Ishchenko,Thomas A. White,Oleksandr Yefanov,Gye Won Han,Qingping Xu,Parker W. de Waal,Kelly Suino-Powell,Sébastien Boutet,Garth J. Williams,Meitian Wang,Dianfan Li,Martin Caffrey,Henry N. Chapman,John C. H. Spence,John C. H. Spence,Petra Fromme,Uwe Weierstall,Uwe Weierstall,Raymond C. Stevens,Raymond C. Stevens,Vadim Cherezov,Karsten Melcher,H. Eric Xu +28 more
TL;DR: The rhodopsin-arrestin crystal structure solved with SFX represents the first near-atomic resolution structure of a GPCR-Arrestin complex, provides structural insights into understanding of arrestin-mediated GPCRs signaling, and demonstrates the great potential of this SFX-XFEL technology for accelerating crystal structure determination of challenging proteins and protein complexes.