Ilme Schlichting

ORCID: 0000-0002-0936-7496
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About
Contact & Profiles
Research Areas
  • Enzyme Structure and Function
  • Advanced X-ray Imaging Techniques
  • Advanced Electron Microscopy Techniques and Applications
  • Photosynthetic Processes and Mechanisms
  • Light effects on plants
  • Biochemical and Molecular Research
  • Photoreceptor and optogenetics research
  • Hemoglobin structure and function
  • Protein Structure and Dynamics
  • Pharmacogenetics and Drug Metabolism
  • X-ray Spectroscopy and Fluorescence Analysis
  • Cancer, Hypoxia, and Metabolism
  • Metal-Catalyzed Oxygenation Mechanisms
  • Cancer-related Molecular Pathways
  • Laser-Plasma Interactions and Diagnostics
  • Computational Drug Discovery Methods
  • Photochromic and Fluorescence Chemistry
  • Colorectal Cancer Treatments and Studies
  • Laser-Matter Interactions and Applications
  • Biochemical Acid Research Studies
  • Microbial Metabolic Engineering and Bioproduction
  • Tryptophan and brain disorders
  • bioluminescence and chemiluminescence research
  • Mass Spectrometry Techniques and Applications
  • Particle Accelerators and Free-Electron Lasers

Max Planck Institute for Medical Research
2015-2024

Max Planck Society
2010-2021

Center for Free-Electron Laser Science
2009-2018

Universität Hamburg
2009-2018

Heidelberg (Poland)
2018

Max Planck Innovation
1999-2013

Cornell University
2010

University of California, Riverside
2007-2010

University of Illinois Urbana-Champaign
1998-2008

Hebrew University of Jerusalem
2008

Members of the cytochrome P450 superfamily catalyze addition molecular oxygen to nonactivated hydrocarbons at physiological temperature—a reaction that requires high temperature proceed in absence a catalyst. Structures were obtained for three intermediates hydroxylation camphor by P450cam with trapping techniques and cryocrystallography. The structure ferrous dioxygen adduct was determined 0.91 angstrom wavelength x-rays; irradiation 1.5 x-rays results breakdown molecule an intermediate...

10.1126/science.287.5458.1615 article EN Science 2000-03-03

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

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

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 demonstrate the use of an X-ray free electron laser synchronized with optical pump to obtain diffraction snapshots from photoactivated states large membrane protein complexes in form nanocrystals flowing a liquid jet.Light-induced changes Photosystem I-Ferredoxin co-crystals were observed at time delays 5 10 µs after excitation.The result correlates microsecond kinetics transfer I ferredoxin.The undocking process that follows leads rearrangements crystals will terminally lead...

10.1364/oe.20.002706 article EN cc-by Optics Express 2012-01-23

We report experimental results on x-ray diffraction of quantum-state-selected and strongly aligned ensembles the prototypical asymmetric rotor molecule 2,5-diiodobenzonitrile using Linac Coherent Light Source. The experiments demonstrate first steps toward a new approach to diffractive imaging distinct structures individual, isolated gas-phase molecules. confirm several key ingredients single experiments: abilities detect count individual scattered photons in shot data, deliver...

10.1103/physrevlett.112.083002 article EN Physical Review Letters 2014-02-28

The plasma dynamics of single mesoscopic Xe particles irradiated with intense femtosecond x-ray pulses exceeding ${10}^{16}\text{ }\text{ }\mathrm{W}/{\mathrm{cm}}^{2}$ from the Linac Coherent Light Source free-electron laser are investigated. Simultaneous recording diffraction patterns and ion spectra allows eliminating influence focal volume intensity particle size distribution. data show that for clusters illuminated pulses, highly charged ionization fragments in a narrow distribution...

10.1103/physrevlett.108.245005 article EN Physical Review Letters 2012-06-15

Optogenetic and chemogenetic control of proteins has revealed otherwise inaccessible facets signaling dynamics. Here, we use light- or ligand-sensitive domains to modulate the structural disorder diverse proteins, thereby generating robust allosteric switches. Sensory were inserted into nonconserved, surface-exposed loops that tight identified computationally as allosterically coupled active sites. Allosteric switches introduced motility (kinases, guanosine triphosphatases, guanine exchange...

10.1126/science.aah3404 article EN Science 2016-12-15

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

Recent advances in synchrotron sources, beamline optics and detectors are driving a renaissance room-temperature data collection. The underlying impetus is the recognition that conformational differences observed functionally important regions of structures determined using crystals kept at ambient as opposed to cryogenic temperature during In addition, measurements enable time-resolved studies eliminate need find suitable cryoprotectants. Since radiation damage limits high-resolution can be...

10.1107/s1399004714026327 article EN Acta Crystallographica Section D Biological Crystallography 2015-01-22
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