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Shinya Saijo

Researcher at KEK

Publications -  26
Citations -  533

Shinya Saijo is an academic researcher from KEK. The author has contributed to research in topics: Protein subunit & ATPase. The author has an hindex of 12, co-authored 26 publications receiving 433 citations. Previous affiliations of Shinya Saijo include Tokyo University of Science.

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Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures

TL;DR: These asymmetric structures represent the first high-resolution view of the rotational mechanism of V1-ATPase from the A3B3 and DF complexes and suggest a binding order in the right-handed rotational orientation in a cooperative manner.
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The crystal structure of plant-specific calcium-binding protein AtCBL2 in complex with the regulatory domain of AtCIPK14.

TL;DR: Structural comparison of the two structures shows that the recognition of CBL by CIPK is performed in a similar manner, but inherent interactions confer binding affinity and specificity.
Journal ArticleDOI

Crystal structure of the central axis DF complex of the prokaryotic V-ATPase.

TL;DR: The crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits, is determined at 2.0-Å resolution.
Proceedings ArticleDOI

Upgrade of small angle x-ray scattering beamline BL-6A at the photon factory

TL;DR: In this paper, a hybrid pixel detector PILATUS3 1M is installed for SAXS, and a pinhole equipped with a micro-ion chamber is available to realize a lower-background and higher-resolution of low angles.
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Mechanism of Catalytic Microtubule Depolymerization via KIF2-Tubulin Transitional Conformation

TL;DR: To elucidate the catalytic mechanism, the transitional KIF2-tubulin complex during MT depolymerization was analyzed through multiple methods, including atomic force microscopy, size-exclusion chromatography, multi-angle light scattering, small-angle X-ray scattering, analytical ultracentrifugation, and mass spectrometry.