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Genji Kurisu

Researcher at Osaka University

Publications -  149
Citations -  5632

Genji Kurisu is an academic researcher from Osaka University. The author has contributed to research in topics: Ferredoxin & Chemistry. The author has an hindex of 33, co-authored 124 publications receiving 4531 citations. Previous affiliations of Genji Kurisu include Osaka Prefecture University & Kyoto Institute of Technology.

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Structure of the Cytochrome b6f Complex of Oxygenic Photosynthesis: Tuning the Cavity

TL;DR: The dimeric b6f complex from the thermophilic cyanobacterium Mastigocladus laminosus reveals a large quinone exchange cavity, stabilized by lipid, in which plastoquinone, a quin one-analog inhibitor, and a novel heme are bound.
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Protein Data Bank: the single global archive for 3D macromolecular structure data

TL;DR: Impacts of the recently developed universal wwPDB OneDep deposition/validation/biocuration system and various methods-specific ww PDB Validation Task Forces on improving the quality of structures and data housed in the PDB Core Archive are described together with current challenges and future plans.
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Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP + reductase

TL;DR: The first crystal structure of the complex between maize leaf Fd and Fd-NADP+ oxidoreductase (FNR) is reported, suggesting that this type of molecular communication not only determines the optimal orientation of the two proteins for electron transfer, but also contributes to the modulation of the enzymatic properties of FNR.
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The 2.8 Å crystal structure of the dynein motor domain

TL;DR: This work reports the most complete structure obtained so far of the 380-kDa motor domain of Dictyostelium discoideum cytoplasmic dynein at 2.8 Å resolution and identifies a long-range allosteric communication pathway between the primary ATPase and the microtubule-binding sites.
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Chlorophyll biosynthesis: spotlight on protochlorophyllide reduction

TL;DR: This review discusses the two fundamentally different mechanisms of Pchlide reduction in photosynthetic organisms, Rhodobacter capsulatus and Rhodob bacteria.