Petra Fromme
· Center Director and Regents Professor, Paul V. Galvin ProfessorArizona State University · Chemistry
Active 1990–2026
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About
Petra Fromme received her B.S. (Vordiplom) and M.S. (Diplom) in biochemistry from the Free University of Berlin, and earned her Ph.D. in chemistry followed by a habilitation in physical chemistry at the Technical University of Berlin. She served as an assistant and associate professor at the Max Volmer Institute before joining Arizona State University as a full professor in the School of Molecular Sciences. In 2012, she was awarded the Paul V. Galvin Professorship, and in 2014, ASU President Michael Crow appointed her as the director of the Center for Applied Structural Discovery. She is also an affiliated member of the Department of Physics and a member of the graduate faculty in the plant biology and biological design graduate program. Professor Fromme's research focuses on the structure-to-function relationship of membrane proteins involved in bioenergy conversion and infectious diseases. Her group studies the structural biochemistry and biophysics of membrane proteins, which are essential for processes such as respiration, photosynthesis, cell communication, and pathogen entry into host cells. The research is interdisciplinary, involving biochemical investigations, molecular biology, spectroscopy, crystallization, X-ray structure analysis, and theoretical studies. She has been a key contributor to the development of serial femtosecond nanocrystallography using high-intensity X-ray Free Electron Lasers (XFEL), enabling the analysis of proteins at unprecedented resolution…
Research topics
- Biology
- Chemistry
- Biochemistry
- Physics
- Computer Science
- Biophysics
- Data Mining
- Crystallography
- Optics
- Materials science
Selected publications
ChAdOx1 interacts with CAR and PF4 with implications for thrombosis with thrombocytopenia syndrome
Science Advances · 2021 · 170 citations
Vaccines derived from chimpanzee adenovirus Y25 (ChAdOx1), human adenovirus type 26 (HAdV-D26), and human adenovirus type 5 (HAdV-C5) are critical in combatting the severe acute respiratory coronavirus 2 (SARS-CoV-2) pandemic. As part of the largest vaccination campaign in history, ultrarare side effects not seen in phase 3 trials, including thrombosis with thrombocytopenia syndrome (TTS), a rare condition resembling heparin-induced thrombocytopenia (HIT), have been observed. This study demonstr…
Science Advances · 2020 · 93 citations
PCC 7521 by single-particle, cryo-electron microscopy to understand its structural and functional differences. Four binding sites occupied by chlorophyll f are proposed. Subtle structural changes enable FRL-adapted PSI to extend light utilization for oxygenic photosynthesis to nearly 800 nm. This structure provides a platform for understanding FRL-driven photosynthesis and illustrates the robustness of adaptive and acclimation mechanisms in nature.
IUCrJ · 2021 · 84 citations
β-lactamase to be followed using time-resolved crystallography in real time. It is shown how a diffusion coefficient in enzyme crystals can be derived directly from the X-ray data, enabling the determination of ligand and enzyme-ligand concentrations at any position in the crystal volume as a function of time. In addition, the structure of the irreversible inhibitor sulbactam bound to the enzyme at a 66 ms time delay after mixing is described. This demonstrates that the EuXFEL can be used as an…
CryoFold: Determining protein structures and data-guided ensembles from cryo-EM density maps
Matter · 2021 · 51 citations
Cryo-electron microscopy (EM) requires molecular modeling to refine structural details from data. Ensemble models arrive at low free-energy molecular structures, but are computationally expensive and limited to resolving only small proteins that cannot be resolved by cryo-EM. Here, we introduce CryoFold - a pipeline of molecular dynamics simulations that determines ensembles of protein structures directly from sequence by integrating density data of varying sparsity at 3-5 Å resolution with coar…
Segmented flow generator for serial crystallography at the European X-ray free electron laser
Nature Communications · 2020 · 44 citations
Serial femtosecond crystallography (SFX) with X-ray free electron lasers (XFELs) allows structure determination of membrane proteins and time-resolved crystallography. Common liquid sample delivery continuously jets the protein crystal suspension into the path of the XFEL, wasting a vast amount of sample due to the pulsed nature of all current XFEL sources. The European XFEL (EuXFEL) delivers femtosecond (fs) X-ray pulses in trains spaced 100 ms apart whereas pulses within trains are currently s…
Recent grants
NSF · $1.6M · 2004–2011
Dynamics of membrane proteins unraveled by time-resolved serial crystallography
NIH · $4.3M · 2010–2025
NIH · $13.5M · 2016
Frequent coauthors
- 154 shared
Henry N. Chapman
Max Planck Institute for the Structure and Dynamics of Matter
- 130 shared
Anton Barty
- 107 shared
Thomas A. White
Deutsches Elektronen-Synchrotron DESY
- 97 shared
Mark S. Hunter
Linac Coherent Light Source
- 89 shared
Sébastien Boutet
- 84 shared
Uwe Weierstall
Arizona State University
- 73 shared
Raimund Fromme
Arizona State University
- 65 shared
John C. H. Spence
Labs
Structural biochemistry and biophysics of membrane proteins
Education
- 1988
Ph.D., Chemistry
Technical University Berlin
- 1985
M.S., Biochemistry
Free University of Berlin
- 1983
B.S., Biochemistry
Free University of Berlin
Awards & honors
- Paul V. Galvin Professorship (2012)
- Director of the Center for Applied Structural Discovery (201…
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