Author

K. Tono

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:protein folding & dynamics· 4 Assay:protein structure· 3 Assay:structural biology· 3 Organism:bacteria (other)· 2 Research Focus:protein structure prediction· 2 Approach:statistical model· 2 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

S. Owada· 6 shared E. Nango· 5 shared R. Tanaka· 5 shared S. Iwata· 5 shared A. Bhowmick· 3 shared A. S. Brewster· 3 shared M. Sugahara· 3 shared N. K. Sauter· 3 shared

Activity by Year

2017-2022 · peak 5/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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6 shared papersBiophysics

S. Owada

Mutual co-authors in cluster

Author profile →

8 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

Inter-subunit coupling enables fast CO2-fixation by reductive carboxylases

H. Demirci, Y. Rao, G. M. Stoffel, B. Vögeli, K. Schell, A. Gomez, A. Batyuk, C. Gati, R. G. Sierra, M. S. Hunter, E. H. Dao, H. I. Ciftci, B. Hayes, F. Poitevin, P. Li, , S. Wakatsuki

This paper investigates the structural and dynamic mechanisms of CO2 fixation by ECRs, revealing inter-subunit coupling that enables fast catalytic activity.

bioRxiv · Feb 23, 2022 · PreprintBiophysics

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

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

Atomic resolution structure of serine protease proteinase K at ambient temperature

T. Masuda, M. Suzuki, S. Inoue, C. Song, T. Nakane, E. Nango, R. Tanaka, K. Tono, Y. Joti, T. Kameshima, T. Hatsui, M. Yabashi, B. Mikami, O. Nureki, K. Numata, , M. Sugahara

The paper reports an atomic resolution structure of proteinase K at ambient temperature using serial femtosecond crystallography, revealing hydrogen atoms, water molecules, and side-chain conformations.

bioRxiv · Feb 21, 2017Biochemistry