Author

F. B. Ertem

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· 6 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Assay:structural biology· 5 Research Focus:protein structure prediction· 3 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

E. Ayan· 7 shared E. Destan· 7 shared A. Shafiei· 5 shared H. DeMirci· 5 shared M. Liang· 5 shared O. Guven· 5 shared R. G. Sierra· 5 shared B. Hayes· 4 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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7 shared papersBiophysics

E. Ayan

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

4D Crystallography Captures Transient IF1-Ribosome Dynamics in Translation Initiation

I. Yapici, E. H. Dao, S. Yokoi, E. Destan, E. Ayan, A. Shafiei Kamel, F. B. Ertem, C. Kulakman, M. Yilmaz, B. Tosun, H. Ciftci, A. Kepceoglu, J. A. Johnson, O. Guven, A. Ergul, , H. DeMirci

This study uses 4D crystallography to capture transient dynamics of IF1 binding to the 30S ribosomal subunit, revealing allostery and interactions during translation initiation.

bioRxiv · Oct 27, 2023 · PreprintBiophysics

Ambient Temperature Bacterial Large Ribosomal Subunit Structure Enabled by Serial Femtosecond X-ray Crystallography

B. Tosun, Y. Rao, E. Destan, E. H. Dao, F. B. Ertem, M. Yilmaz, I. Yapici, M. Gul, E. Ayan, J. A. Johnson, A. Shafiei, C. Kulakman, B. Hayes, M. Liang, C. H. Yoon, , H. DeMirci

This study determines the structure of the 50S ribosomal subunit from Thermus thermophilus at ambient temperature using serial femtosecond X-ray crystallography, revealing new dynamics and antibiotic binding sites.

bioRxiv · Oct 24, 2023 · PreprintBiophysics

Rapid and Efficient Ambient Temperature X-ray Crystal Structure Determination at Turkish Light Source

M. Gul, E. Ayan, E. Destan, J. A. Johnson, A. Shafiei, A. Kepceoglu, M. Yilmaz, F. B. Ertem, I. Yapici, B. Tosun, N. Baldir, N. Tokay, Z. Nergiz, G. Karakadioglu, S. S. Paydos, , H. DeMirci

The paper introduces a plate-reader module for rapid ambient temperature X-ray crystallography at a home source and reports the first lysozyme structure determined at Turkish DeLight.

bioRxiv · Oct 12, 2022 · PreprintBiophysics

Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source: Turkish DeLight

N. Atalay, E. K. Akcan, M. Gul, E. Ayan, E. Destan, F. B. Ertem, N. Tokay, B. Cakilkaya, Z. Nergiz, G. Karakadioglu, A. Kepceoglu, I. Yapici, B. Tosun, N. Baldir, G. Yildirim, , Kati

The paper describes the setup and application of a new X-ray crystallography facility in Turkey for structural analysis of biomacromolecules using lysozyme as a model.

bioRxiv · Sep 3, 2022Biophysics

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

Structural insight into host plasma membrane association and assembly of HIV-1 Matrix protein

H. Ciftci, H. Tateishi, K. Koiwai, R. Koga, K. Anraku, K. Monde, C. Dag, E. Destan, B. Yuksel, E. Ayan, G. Yildirim, M. Yigin, F. B. Ertem, A. Shafiei, O. Guven, , H. DeMirci

This study presents crystal structures of HIV-1 MA domain bound to IP6, revealing its binding mode and interaction with PIP2, providing insights into virion assembly.

bioRxiv · Feb 21, 2021 · PreprintMicrobiology

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