Author

D. von Stetten

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· 4 Biochemistry· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:protein folding & dynamics· 5 Assay:structural biology· 5 Assay:cryo-EM· 2 Organism:human· 2 Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:protein structure· 1

Frequent Co-Authors

P. Mehrabi· 4 shared D. Axford· 3 shared E. C. Schulz· 3 shared F. Tellkamp· 3 shared H. Schikora· 3 shared A. Prester· 2 shared A. R. Pearson· 2 shared C. E. Hatton· 2 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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4 shared papersBiophysics

P. Mehrabi

Mutual co-authors in cluster

Author profile →

7 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

An ultraviolet-driven rescue pathway for oxidative stress to eye lens protein human gamma-D crystallin.

J. A. Hill, Y. R. Nyathi, S. Horrell, D. von Stetten, D. Axford, R. L. Owen, G. S. Beddard, A. R. Pearson, H. M. Ginn, B. A. Yorke

The paper identifies a UV-induced redox switch mechanism in human gamma-D crystallin that may rescue oxidative damage.

bioRxiv · Aug 25, 2023Biochemistry

A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron binding protein FutA from Prochlorococcus

R. Bolton, M. M. Machelett, J. Stubbs, D. Axford, N. Caramello, L. Catapano, M. Maly, M. J. Rodrigues, C. Cordery, G. J. Tizzard, F. MacMillan, S. Engilberge, D. von Stetten, T. Tosha, H. Sugimoto, , I. Tews

This paper reveals a redox switch in the cyanobacterial iron binding protein FutA that allows it to bind both Fe(II) and Fe(III) ions through structural analysis.

bioRxiv · May 23, 2023 · PreprintBiophysics

Millisecond cryo-trapping by the spitrobot crystal plunger simplifies time-resolved crystallography

P. Mehrabi, S. Sung, D. von Stetten, A. Prester, C. E. Hatton, S. Kleine-Doepke, A. Berkes, G. Gore, J.-P. Leimkohl, H. Schikora, M. Kollewe, H. Rohde, M. Wilmanns, F. Tellkamp, E. C. Schulz

The paper introduces a device called spitrobot that enables millisecond time-resolved crystallography by cryo-trapping reaction intermediates.

bioRxiv · Sep 20, 2022 · PreprintBiophysics

Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging

B. Norton-Baker, P. Mehrabi, A. O. Kwok, K. W. Roskamp, M. A. Spague-Piercy, D. von Stetten, R. J. D. Miller, R. W. Martin

This study reports six crystal structures of deamidated γS-crystallin variants, showing increased instability, aggregation, and disulfide bond formation, suggesting deamidation accelerates oxidative aging in the human lens.

Structure · May 1, 2022Peer-reviewedBiochemistry

Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography

E. C. Schulz, A. Prester, D. von Stetten, G. Gore, C. E. Hatton, K. Bartels, J.-P. Leimkohl, H. Schikora, H. M. Ginn, F. Tellkamp, P. Mehrabi

The paper introduces an environmental enclosure for serial crystallography to study enzyme kinetics across temperatures, showing temperature-dependent modulation in two enzymes.

bioRxiv · Nov 7, 2021Biophysics

Serial femtosecond and serial synchrotron crystallography yield data of equivalent quality: a systematic comparison

P. Mehrabi, R. Buecker, G. Bourenkov, H. Ginn, D. von Stetten, H. M. Mueller-Werkmeister, A. Kuo, T. Morizumi, B. Eger, W.-L. Ou, S. Oghbaey, A. Sarracini, J. Besaw, O. Pare-Labrosse, S. Meier, , R. J. D. Miller

This study compares data quality from serial femtosecond and serial synchrotron crystallography for two proteins, finding equivalent quality regardless of radiation source.

bioRxiv · Aug 21, 2020Biophysics