Author

S. Owada

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· 5 Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:protein folding & dynamics· 5 Assay:structural biology· 3 Organism:bacteria (other)· 2 Assay:protein structure· 2 Assay:cryo-EM· 1 Organism:E. coli· 1 Assay:fluorescence / live-cell microscopy· 1

Frequent Co-Authors

K. Tono· 6 shared E. Nango· 5 shared R. Tanaka· 5 shared S. Iwata· 5 shared T. Tanaka· 4 shared A. Bhowmick· 3 shared A. S. Brewster· 3 shared N. K. Sauter· 3 shared

Activity by Year

2019-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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6 shared papersBiophysics

K. Tono

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

ULTRAFAST STRUCTURAL CHANGES DIRECT THE FIRST MOLECULAR EVENTS OF VISION

T. Gruhl, T. Weinert, M. Rodrigues, C. J. Milne, G. Ortolani, K. Nass, E. Nango, S. Sen, P. J. Johnson, C. Cirelli, A. Furrer, S. Mous, P. Skopintsev, D. James, F. Dworkowski, , Scher

This study uses ultrafast crystallography to reveal how photoactivated retinal initiates structural changes in rhodopsin, leading to GPCR activation and vision.

bioRxiv · Oct 14, 2022 · PreprintBiochemistry

Rational control of structural off-state heterogeneity in a photoswitchable fluorescent protein provides switching contrast enhancement

V. Adam, K. Hadjidemetriou, N. Jensen, R. L. Shoeman, J. Woodhouse, A. Aquila, A.-S. Banneville, T. R. M. Barends, V. Bezchastnov, S. Boutet, M. Byrdin, M. Cammarata, S. Carbajo, N.-E. Christou, N. Coquelle, , Za

This paper enhances switching contrast in photoswitchable fluorescent proteins by modifying the V151 side chain, improving performance in RESOLFT nanoscopy.

ChemPhysChem · Aug 12, 2022Peer-reviewedBiophysics

Mapping Protein Dynamics at High-Resolution with Temperature-Jump X-ray Crystallography

A. M. Wolff, E. Nango, I. D. Young, A. S. Brewster, M. Kubo, T. Nomura, M. Sugahara, S. Owada, B. A. Barad, K. Ito, A. Bhowmick, S. Carbajo, T. Hino, J. M. Holton, D. Im, , M. C. Thompson

This study uses temperature-jump X-ray crystallography to observe atomic-scale protein motions in lysozyme, showing how vibrations evolve into functional movements and how inhibitors alter these dynamics.

bioRxiv · Jun 10, 2022Biophysics

Redox-controlled structural reorganization and flavin strain within the ribonucleotide reductase R2b-NrdI complex monitored by serial femtosecond crystallography

J. John, O. Aurelius, V. Srinivas, I.-S. Kim, A. Bhowmick, P. S. Simon, M. Dasgupta, C. Pham, S. Gul, K. D. Sutherlin, P. Aller, A. Butryn, A. M. Orville, M. H. Cheah, S. Owada, , M. Hogbom

The paper uses serial femtosecond crystallography to study redox-induced structural changes in the R2b-NrdI complex, revealing flavin strain and its role in superoxide generation.

bioRxiv · Apr 14, 2022Biochemistry

High-resolution Crystal Structures of Transient Intermediates in the Phytochrome Photocycle

M. Carrillo, S. Pandey, J. Sanchez, M. Noda, I. Poudyal, L. Aldama, T. N. Malla, E. Claesson, W. Yuan Wahlgreen, D. Feliz, V. Srajer, M. Maj, L. Castillon, S. Iwata, E. Nango, , M. Schmidt

The paper captures high-resolution crystal structures of transient phytochrome intermediates to elucidate the structural changes during the Pr-to-Pfr photocycle.

bioRxiv · Sep 16, 2020Biophysics

The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

E. Claesson, W. Yuan Wahlgren, H. Takala, S. Pandey, L. Castillon, V. Kuznetsova, L. Henry, M. Carrillo, M. Panman, J. Kubel, R. Nanekar, L. Isaksson, A. Nimmrich, A. Cellini, D. Morozov, , S. Westenhoff

This study captures the structural changes in bacterial phytochrome proteins after light exposure using femtosecond X-ray crystallography, revealing key molecular movements involved in the photoresponse.

bioRxiv · Oct 1, 2019Biophysics

Comparing serial X-ray crystallography and microcrystal electron diffraction (MicroED) as methods for routine structure determination from small macromolecular crystals

A. M. Wolff, I. D. Young, R. G. Sierra, A. S. Brewster, M. W. Martynowycz, E. Nango, M. Sugahara, T. Nakane, K. Ito, A. Aquila, A. Bhowmick, J. T. Biel, S. Carbajo, A. E. Cohen, S. Cortez, , M. C. Thompson

This study compares serial X-ray crystallography and MicroED for determining structures from small macromolecular crystals, highlighting their strengths and challenges.

bioRxiv · Sep 12, 2019Biophysics