Petra Fromme

ORCID: 0000-0003-0953-4909
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About
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Research Areas
  • Photosynthetic Processes and Mechanisms
  • Enzyme Structure and Function
  • Photoreceptor and optogenetics research
  • Advanced Electron Microscopy Techniques and Applications
  • Advanced X-ray Imaging Techniques
  • Spectroscopy and Quantum Chemical Studies
  • Protein Structure and Dynamics
  • Mitochondrial Function and Pathology
  • Biochemical and Molecular Research
  • Receptor Mechanisms and Signaling
  • Crystallization and Solubility Studies
  • Algal biology and biofuel production
  • Mass Spectrometry Techniques and Applications
  • ATP Synthase and ATPases Research
  • RNA and protein synthesis mechanisms
  • X-ray Spectroscopy and Fluorescence Analysis
  • Light effects on plants
  • Bacteriophages and microbial interactions
  • Metal-Catalyzed Oxygenation Mechanisms
  • Microfluidic and Capillary Electrophoresis Applications
  • Porphyrin and Phthalocyanine Chemistry
  • Metalloenzymes and iron-sulfur proteins
  • Origins and Evolution of Life
  • X-ray Diffraction in Crystallography
  • Advanced Fluorescence Microscopy Techniques

Arizona State University
2016-2025

Argonne National Laboratory
2016-2019

Max Planck Institute for Nuclear Physics
2018

Universität Hamburg
2016

Deutsches Elektronen-Synchrotron DESY
2016

Center for Free-Electron Laser Science
2016

Physical Sciences (United States)
2013-2014

Statistics Finland
2012

European Synchrotron Radiation Facility
2008

Lawrence Berkeley National Laboratory
2002-2006

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

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

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
Max O. Wiedorn Dominik Oberthür Richard Bean Robin Schubert N. Werner and 95 more Brian Abbey Martin Aepfelbacher Luigi Adriano A. Allahgholi Nasser Al-Qudami Jakob Andreasson Steve Aplin Salah Awel Kartik Ayyer S. Bajt Imrich Barák Sadia Bari Johan Bielecki Sabine Botha Djelloul Boukhelef W. Brehm Sándor Brockhauser Igor Cheviakov Matthew A. Coleman Francisco Cruz-Mazo Cyril Danilevski Connie Darmanin R. Bruce Doak M. Domaracký Katerina Dörner Yang Du Hans Fangohr Holger Fleckenstein Matthias Frank Petra Fromme Alfonso M. Gañán‐Calvo Y. Gevorkov Klaus Giewekemeyer Helen M. Ginn H. Graafsma Rita Graceffa D. Greiffenberg Lars Gumprecht P. Göttlicher János Hajdu Steffen Hauf Michaël Heymann Susannah Holmes Daniel A. Horke Mark S. Hunter Siegfried Imlau Alexander Kaukher Yoonhee Kim A. Klyuev J. Knoška Boštjan Kobe Manuela Kuhn Christopher Kupitz Jochen Küpper J. M. Rudolph Torsten Laurus K. Le Cong Romain Letrun P. Lourdu Xavier Luis Maia Filipe R. N. C. Maia Valerio Mariani M. Messerschmidt Markus Metz D. Mezza Thomas Michelat Grant Mills Diana C. F. Monteiro Andrew J. Morgan Kerstin Mühlig Anna Munke Astrid Münnich Julia Nette K. Nugent Theresa Nuguid Allen M. Orville Suraj Pandey Gisel E. Peña Murillo Pablo Villanueva‐Perez Jennifer Poehlsen Gianpietro Previtali Lars Redecke Winnie Maria Riekehr Holger Rohde Adam Round Tatiana Safenreiter Iosifina Sarrou Tokushi Sato Marius Schmidt B. Schmitt Robert Schönherr Joachim Schulz Jonas A. Sellberg M. Seibert Carolin Seuring

Abstract The new European X-ray Free-Electron Laser is the first free-electron laser capable of delivering pulses with a megahertz inter-pulse spacing, more than four orders magnitude higher previously possible. However, to date, it has been unclear whether would indeed be possible measure high-quality diffraction data at pulse repetition rates. Here, we show that structures can obtained using currently available operating conditions XFEL. We present two complete sets, one from well-known...

10.1038/s41467-018-06156-7 article EN cc-by Nature Communications 2018-09-26
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