Sébastien Boutet

ORCID: 0000-0003-3928-1244
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About
Contact & Profiles
Research Areas
  • Advanced X-ray Imaging Techniques
  • Enzyme Structure and Function
  • Advanced Electron Microscopy Techniques and Applications
  • X-ray Spectroscopy and Fluorescence Analysis
  • Photosynthetic Processes and Mechanisms
  • Laser-Plasma Interactions and Diagnostics
  • Photoreceptor and optogenetics research
  • Protein Structure and Dynamics
  • Particle Accelerators and Free-Electron Lasers
  • Spectroscopy and Quantum Chemical Studies
  • Crystallography and Radiation Phenomena
  • Laser-Matter Interactions and Applications
  • Advanced Chemical Physics Studies
  • Advanced Fluorescence Microscopy Techniques
  • Receptor Mechanisms and Signaling
  • Biochemical and Molecular Research
  • nanoparticles nucleation surface interactions
  • Viral Infectious Diseases and Gene Expression in Insects
  • Mass Spectrometry Techniques and Applications
  • High-pressure geophysics and materials
  • Atomic and Molecular Physics
  • Diamond and Carbon-based Materials Research
  • Insect and Pesticide Research
  • Laser-induced spectroscopy and plasma
  • Hemoglobin structure and function

Linac Coherent Light Source
2016-2025

SLAC National Accelerator Laboratory
2016-2025

Renault (France)
2021

Fermi National Accelerator Laboratory
2021

Menlo School
2009-2019

Bioengineering Center
2019

SPring-8
2008-2019

Kyoto University
2019

High Energy Accelerator Research Organization
2019

Deutsches Elektronen-Synchrotron DESY
2017

10.1038/nature09748 article EN Nature 2011-02-01

Size Matters Less X-ray crystallography is a central research tool for uncovering the structures of proteins and other macromolecules. However, its applicability typically requires growth large crystals, in part because sufficient number molecules must be present lattice sample to withstand x-ray—induced damage. Boutet et al. (p. 362 , published online 31 May) now demonstrate that intense x-ray pulses emitted by free-electron laser source can yield data few enough exposures uncover...

10.1126/science.1217737 article EN Science 2012-06-01

In the five years since achieving first light at Linac Coherent Light Source, transformative studies have been conducted in a new regime with femtosecond pulses of short wavelength, high intensity x rays. This article summarizes these results atomic, molecular and optical physics; condensed matter extreme density, temperature pressure conditions; chemistry soft matter; biological structure dynamics. each areas, perspectives for future research are discussed.

10.1103/revmodphys.88.015007 article EN publisher-specific-oa Reviews of Modern Physics 2016-03-09

Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics biomolecules. We used microcrystals photoactive yellow protein (a bacterial blue light photoreceptor) as a model system and obtained high-resolution, time-resolved difference density maps excellent quality with strong features; these allowed determination structures reaction intermediates to resolution 1.6 angstroms. Our results open way study...

10.1126/science.1259357 article EN Science 2014-12-04

X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) individual 50-femtosecond-duration pulses to minimize obtained a room-temperature structure human serotonin receptor using sub-10-micrometer microcrystals grown in mimetic matrix known as lipidic cubic phase....

10.1126/science.1244142 article EN Science 2013-12-19

The Trypanosoma brucei cysteine protease cathepsin B (TbCatB), which is involved in host protein degradation, a promising target to develop new treatments against sleeping sickness, fatal disease caused by this protozoan parasite. structure of the mature, active form TbCatB has so far not provided sufficient information for design safe and specific drug T. brucei. By combining two recent innovations, vivo crystallization serial femtosecond crystallography, we obtained room-temperature 2.1...

10.1126/science.1229663 article EN Science 2012-11-30

Visualizing a response to light Many biological processes depend on detecting and responding light. The is often mediated by structural change in protein that begins when absorption of photon causes isomerization chromophore bound the protein. Pande et al. used x-ray pulses emitted free electron laser source conduct time-resolved serial femtosecond crystallography time range 100 fs 3 ms. This allowed for real-time tracking trans-cis photoactive yellow associated changes Science , this issue p. 725

10.1126/science.aad5081 article EN Science 2016-05-06

Intense femtosecond x-ray pulses produced at the Linac Coherent Light Source (LCLS) were used for simultaneous diffraction (XRD) and emission spectroscopy (XES) of microcrystals photosystem II (PS II) room temperature. This method probes overall protein structure electronic Mn4CaO5 cluster in oxygen-evolving complex PS II. XRD data are presented from both dark state (S1) first illuminated (S2) Our XRD-XES study shows that crystals intact during our measurements LCLS, not only with respect to...

10.1126/science.1234273 article EN Science 2013-02-15

The hemoprotein myoglobin is a model system for the study of protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve ultrafast structural changes in carbonmonoxy complex upon photolysis Fe-CO bond. Structural appear throughout within 500 femtoseconds, with C, F, and H helices moving away from heme cofactor E A toward it. These collective movements are predicted by hybrid quantum mechanics/molecular mechanics simulations. Together...

10.1126/science.aac5492 article EN Science 2015-09-11

We present results from experiments at the Linac Coherent Light Source (LCLS) demonstrating that serial femtosecond crystallography (SFX) can be performed to high resolution (~2.5 Å) using protein microcrystals deposited on an ultra-thin silicon nitride membrane and embedded in a preservation medium room temperature. Data acquired acquisition rate x-ray free electron laser sources overcome radiation damage, while sample consumption is dramatically reduced compared flowing jet methods....

10.1038/srep06026 article EN cc-by-nc-nd Scientific Reports 2014-08-12

Intense femtosecond x-ray pulses from free-electron laser sources allow the imaging of individual particles in a single shot. Early experiments at Linac Coherent Light Source (LCLS) have led to rapid progress field and, so far, coherent diffractive images been recorded biological specimens, aerosols, and quantum systems with few-tens-of-nanometers resolution. In March 2014, LCLS held workshop discuss scientific technical challenges for reaching ultimate goal atomic resolution single-shot...

10.1063/1.4918726 article EN cc-by Structural Dynamics 2015-04-21
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