Author

S. Botha

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1 Organism:virus· 1

Frequent Co-Authors

A. Barty· 2 shared A. Batyuk· 2 shared A. Tolstikova· 2 shared B. Hayes· 2 shared B. Yuksel· 2 shared C. Dag· 2 shared C. H. Yoon· 2 shared E. Ayan· 2 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersBiophysics

A. Barty

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Light-induced Trpin/Metout switching during BLUF domain activation in ATP-bound photoactivatable adenylate cyclase OaPAC

A. Chretien, M. F. Nagel, S. Botha, R. de Wijn, L. Brings, K. Doerner, H. Han, J. C. P. Koliyadu, R. Letrun, A. Round, T. Sato, C. Schmidt, R.-C. Secareanu, D. von Stetten, M. Vakili, , R. Schubert

This study investigates the light-induced structural changes in OaPAC's BLUF domain, revealing a Trpin/Metout transition and conformational shifts during ATP activation.

bioRxiv · Sep 5, 2023Biochemistry

Cooperative Allostery and Structural Dynamics of Streptavidin at Cryogenic- and Ambient-temperature

E. Ayan, B. Yuksel, E. Destan, F. B. Ertem, G. Yildirim, M. Eren, O. M. Yefanov, A. Barty, A. Tolstikova, G. K. Ketawala, S. Botha, E. H. Dao, B. Hayes, M. Liang, M. H. Seaberg, , H. DeMirci

The paper presents two apo-streptavidin structures at different temperatures and reveals cooperative allostery through water-mediated interactions.

bioRxiv · Sep 23, 2021Biophysics

Near-Physiological-Temperature Serial Femtosecond X-ray Crystallography Reveals Novel Conformations of SARS-CoV-2 Main Protease Active Site for Improved Drug Repurposing

S. Durdagi, C. Dag, B. Dogan, M. Yigin, T. Avsar, C. Buyukdag, I. Erol, F. B. Ertem, S. Calis, G. Yildirim, M. Orhan, O. Guven, B. Aksoydan, E. Destan, K. Sahin, , Sn

The paper determines two apo structures of SARS-CoV-2 main protease at near-physiological temperature using SFX and uses molecular simulations to analyze inhibitor binding for drug repurposing.

bioRxiv · Sep 9, 2020Biophysics