Author

Cecilia Maria Casadei

Lund UniversityORCID 0000-0002-8246-9667Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biophysics· 2 Biochemistry· 1

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· 2 shared Anna KoczurowskaiD· 2 shared Ayesha Asghar· 2 shared Bence OlasziD· 2 shared Dean Lang· 2 shared Jie Nan· 2 shared Larissa Lopes CavalcanteiD· 2 shared M. WisniewskaiD· 2 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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2 shared papersBiophysics

Aleksandra SoleckaORCID

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3 papers

Recent·Most cited

Injector-based pump-probe serial synchrotron crystallography of CrPhotLOV1 at the MicroMAX beamline

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

This paper establishes a robust workflow for injector-based pump-probe TR-SSX at the MicroMAX beamline to study CrPhotLOV1 structural dynamics.

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

Anaerobic time-resolved serial crystallography captures CO dissociation and rebinding in oxygen-sensitive -hydrogenase

Ivan Voloshyn, Robin Stipp, Lukas Grunewald, Laura Angela Kiesewetter, Samuel L. Rose, Shibom Basu, Cecilia Maria Casadei, Monika Bjelčić, Daniele de Sanctis, Sebastian Westenhoff, Moritz Senger

This study uses anaerobic time-resolved serial crystallography to capture CO dissociation and rebinding in [FeFe]-hydrogenase, revealing a rigid catalytic architecture.

bioRxiv · Jul 23, 2026 · PreprintBiochemistry