Author

L. Foucar

Max Planck Institute for Medical Research

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Biochemistry· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Assay:structural biology· 2 Approach:biophysical modeling· 1 Organism:E. coli· 1 Assay:fluorescence / live-cell microscopy· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

A. GoreliD· 4 shared M. HilpertiD· 4 shared Elena A. AndreevaiD· 2 shared Elke De ZitteriD· 2 shared G. Schiro· 2 shared Gabriela Nass Kovacs· 2 shared Giorgio SchiròiD· 2 shared Ilme SchlichtingiD· 2 shared

Activity by Year

2022-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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4 shared papersBiophysics

A. GorelORCID

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structural basis of the two-photon photoactivation mechanism of orange carotenoid protein

Rory Munro, Elena A. Andreeva, Elisabeth Hartmann, Quentin Goor, Hosni El Zein, Stanisław Niziński, Adjélé Wilson, Elke De Zitter, Grégory Effantin, Nicolas Coquelle, Ninon Zala, Martin V. Appleby, Shira Bar-Zvi, Camila Bacellar, Emma V. Beale, , Jacques‐Philippe Colletier

The paper elucidates the structural basis of the two-photon photoactivation mechanism of orange carotenoid protein using a combination of structural and biochemical methods.

bioRxiv · May 10, 2026 · PreprintBiochemistry

Influence of pump laser fluence on ultrafast structural changes in myoglobin

T. R. M. Barends, S. Bhattacharyya, A. Gorel, G. Schiro, C. Bacellar, C. Cirelli, J.-P. Colletier, L. Foucar, M. L. Gruenbein, E. Hartmann, M. Hilpert, P. Johnson, M. Kloos, G. Knopp, B. Marekha, , I. Schlichting

This study shows that varying pump laser fluence in TR-SFX experiments affects structural dynamics and coherent oscillations in myoglobin, highlighting the need for linear photoexcitation in ultrafast studies.

bioRxiv · Nov 22, 2022 · PreprintBiophysics

Rational control of structural off-state heterogeneity in a photoswitchable fluorescent protein provides switching contrast enhancement

V. Adam, K. Hadjidemetriou, N. Jensen, R. L. Shoeman, J. Woodhouse, A. Aquila, A.-S. Banneville, T. R. M. Barends, V. Bezchastnov, S. Boutet, M. Byrdin, M. Cammarata, S. Carbajo, N.-E. Christou, N. Coquelle, , Za

This paper enhances switching contrast in photoswitchable fluorescent proteins by modifying the V151 side chain, improving performance in RESOLFT nanoscopy.

ChemPhysChem · Aug 12, 2022Peer-reviewedBiophysics

De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals

Guillaume Tetreau, Michael R. Sawaya, Elke De Zitter, Elena A. Andreeva, Anne‐Sophie Banneville, Natalie A. Schibrowsky, Nicolas Coquelle, Aaron S. Brewster, Marie Luise Grünbein, Gabriela Nass Kovacs, Mark S. Hunter, Marco Kloos, Raymond G. Sierra, Giorgio Schirò, Pei Qiao, , Jacques‐Philippe Colletier

The paper determines the structures of Cry11Aa and Cry11Ba toxins using serial femtosecond crystallography, revealing new insights into their in vivo crystallization patterns and toxicity.

Nature Communications · Jul 28, 2022Peer-reviewedMolecular Biology