Author

Ran Ke

Jagiellonian UniversityORCID 0009-0002-6957-2237Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:protein structure· 2 Research Focus:protein structure prediction· 2 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1

Frequent Co-Authors

Aleksandra SoleckaiD· 3 shared Anna KoczurowskaiD· 3 shared Ayesha Asghar· 3 shared Bence OlasziD· 3 shared M. WisniewskaiD· 3 shared Madan Kumar Shankar· 3 shared Magdalena PachotaiD· 3 shared Przemysław NogłyiD· 3 shared

Activity by Year

2026-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiophysics

Aleksandra SoleckaORCID

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3 papers

Recent·Most cited

Room-temperature light-state structure of the AsLOV2-Rac1 optogenetic actuator by sheet-on-sheet serial femtosecond crystallography

Magdalena Pachota, M. Wisniewska, Madan Kumar Shankar, Martin V. Appleby, Anna Koczurowska, Ayesha Asghar, Michał Kępa, Ran Ke, Aleksandra Solecka, Teresa Durán Kobylecka, Bence Olasz, Sandra TM Mous, John H. Beale, Guillaume Gotthard, Przemysław Nogły

The paper reports room-temperature light-state structures of AsLOV2-Rac1 using serial femtosecond crystallography, revealing structural changes upon light activation.

bioRxiv · Oct 30, 2026 · PreprintBiophysics

Photoactivatable Rac1: a photosensor tilt by time-resolved crystallography and a partially open switch I when GDP-bound

Magdalena Pachota, Madan Kumar Shankar, M. Wisniewska, Anna Koczurowska, Cecilia Maria Casadei, Aleksandra Solecka, Sofia M. Kapetanaki, Bence Olasz, Larissa Lopes Cavalcante, Ran Ke, Dean Lang, Monika Bjelčić, Ayesha Asghar, Mirko Milas, Thomas Ursby, , Przemysław Nogły

This paper uses time-resolved crystallography to visualize how light activates Rac1 by tilting the LOV2 domain and partially opening switch I when GDP-bound.

bioRxiv · Oct 28, 2026 · PreprintBiophysics

Covalent bond formation caught in a LOV photoreceptor

Bence Olasz, Guillaume Gotthard, Probal Nag, María González-Viegas, Sandra TM Mous, Anna Koczurowska, Philip J. M. Johnson, Tokushi Sato, Madan Kumar Shankar, Maximilian Wranik, Aleksandra Solecka, Diogo V. M. Melo, Ran Ke, Daniel James, Karol Nass, , Przemysław Nogły

This paper resolves the mechanism of covalent bond formation in a LOV photoreceptor using time-resolved crystallography and spectroscopy, revealing a water-mediated proton transfer that accelerates the reaction by fourteen orders of magnitude.

bioRxiv · Aug 6, 2026 · PreprintBiophysics