東北大学研究者紹介

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ハマグチ　タスク

濵口　祐

Tasuku Hamaguchi

所属

多元物質科学研究所　有機・生命科学研究部門　生物分子機能計測研究分野

職名

准教授

学位

博士（理学）（大阪市立大学）
修士（理学）（大阪市立大学）

researchmap

https://researchmap.jp/read0153256

J-GLOBAL ID

201001003804108546

経歴 5

2022年4月～継続中

東北大学　多元物質科学研究所　准教授
2017年5月～ 2022年3月

特定国立研究開発法人理化学研究所　放射光科学研究センター生体機構研究グループ　研究員
2013年4月～ 2017年3月

大阪市立大学　理学部細胞機能学研究室　特任助教
2012年4月～ 2013年3月

大阪市立大学　理学部生体高分子機能学研究室　特任講師
2010年4月～ 2012年3月

大阪市立大学　理学部生体高分子機能学研究室　特任助教

学歴 4

大阪市立大学大学院　理学研究科　生物地球系専攻

2007年4月～ 2010年3月
大阪市立大学大学院　理学研究科　生物地球系専攻

2005年4月～ 2007年3月
大阪市立大学　理学部　生物学科

2001年4月～ 2005年3月
和歌山県立新宮高校

1998年4月～ 2001年3月

所属学協会 5

日本生物物理学会

2013年～継続中
日本マイコプラズマ学会

2013年4月～ 2017年3月
日本細菌学会

2013年4月～ 2017年3月
日本農芸化学会

2005年4月～ 2013年3月
日本生化学会

2005年4月～ 2013年3月

研究キーワード 8

膜タンパク質
単粒子解析
クライオ電子顕微鏡
電子顕微鏡
AFM
Mycoplasma
タンパク質構造解析
糖鎖遊離酵素

研究分野 1

ライフサイエンス / 形態、構造 / タンパク質の構造解析

受賞 2

理研研究奨励賞（桜舞賞）

2021年3月　理化学研究所　クライオ電子顕微鏡を用いた高分解能単粒子構造解析
日本マイコプラズマ学術集会優秀発表賞

2015年5月　日本マイコプラズマ学会

論文 48

Versatile Nanoparticle Capsule Formation With Enhanced Encapsulation Efficiency via Solute‐Induced Liquid–Liquid Phase Separation 国際誌査読有り

Takehiro Yachi, Honoka Watanabe, Rumi Niwa, Daisuke Unabara, Tasuku Hamaguchi, Yusuke Yonamine, Koji Yonekura, Kuniharu Ijiro, Hideyuki Mitomo

Small　2502573　2025年7月
出版者・発行元： Wiley-VCH GmbH
DOI： 10.1002/smll.202502573 　
Dimeric assembly of F1-like ATPase for the gliding motility of Mycoplasma

Takuma TOYONAGA, Takayuki KATO, Akihiro KAWAMOTO, Tomoko MIYATA, Keisuke KAWAKAMI, Junso FUJITA, Tasuku HAMAGUCHI, Keiichi NAMBA, Makoto MIYATA

Science Advances　11　(9)　2025年2月26日
出版者・発行元： American Association for the Advancement of Science's (AAAS)
DOI： 10.1126/sciadv.adr9319 　
Assembly Formation of P65, an Intrinsically Disordered Protein Involved in Gliding Machinery of Mycoplasma pneumoniae

Masaru Yabe, Takuma Toyonaga, Miki Kinoshita, Yukio Furukawa, Tasuku Hamaguchi, Yuhei O Tahara, Munehito Arai, Katsumi Imada, Makoto Miyata

Biomolecules　2025年2月17日

DOI： 10.20944/preprints202502.1200.v1 　
Structure of endothelin ETB receptor–Gi complex in a conformation stabilized by unique NPxxL motif

Kazutoshi Tani, Saori Maki-Yonekura, Ryo Kanno, Tatsuki Negami, Tasuku Hamaguchi, Malgorzata Hall, Akira Mizoguchi, Bruno M. Humbel, Tohru Terada, Koji Yonekura, Tomoko Doi

Communications Biology　2024年10月16日

DOI： 10.1038/s42003-024-06905-z 　
The structure of PSI-LHCI from Cyanidium caldarium provides evolutionary insights into conservation and diversity of red-lineage LHCs

Koji Kato, Tasuku Hamaguchi, Minoru Kumazawa, Yoshiki Nakajima, Kentaro Ifuku, Shunsuke Hirooka, Yuu Hirose, Shin-ya Miyagishima, Takehiro Suzuki, Keisuke Kawakami, Naoshi Dohmae, Koji Yonekura, Jian-Ren Shen, Ryo Nagao

Proceedings of the National Academy of Sciences　121　(11)　2024年3月5日
出版者・発行元： Proceedings of the National Academy of Sciences
DOI： 10.1073/pnas.2319658121 　

ISSN：0027-8424

eISSN：1091-6490

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Light-harvesting complexes (LHCs) are diversified among photosynthetic organisms, and the structure of the photosystem I-LHC (PSI-LHCI) supercomplex has been shown to be variable depending on the species of organisms. However, the structural and evolutionary correlations of red-lineage LHCs are unknown. Here, we determined a 1.92-Å resolution cryoelectron microscopic structure of a PSI-LHCI supercomplex isolated from the red alga Cyanidium caldarium RK-1 (NIES-2137), which is an important taxon in the Cyanidiophyceae. We subsequently investigated the correlations of PSI-LHCIs from different organisms through structural comparisons and phylogenetic analysis. The PSI-LHCI structure obtained shows five LHCI subunits surrounding a PSI-monomer core. The five LHCIs are composed of two Lhcr1s, two Lhcr2s, and one Lhcr3. Phylogenetic analysis of LHCs bound to PSI in the red-lineage algae showed clear orthology of LHCs between C. caldarium and Cyanidioschyzon merolae , whereas no orthologous relationships were found between C. caldarium Lhcr1–3 and LHCs in other red-lineage PSI-LHCI structures. These findings provide evolutionary insights into conservation and diversity of red-lineage LHCs associated with PSI.
クライオ電子顕微鏡による高分子の局所構造観察招待有り

浜口祐

高分子　72　(12)　595-598　2023年12月
出版者・発行元：公益社団法人高分子学会
Formation of Polyion Complex Aggregate Formed from a Cationic Block Copolymer and Anionic Polysaccharide 査読有り

Kazushi Ogata, Mineo Hashizume, Rintaro Takahashi, Tasuku Hamaguchi, Hiroshi Jinnai, Shin-ichi Yusa

Langmuir　39　(46)　16484-16493　2023年11月10日
出版者・発行元： American Chemical Society (ACS)
DOI： 10.1021/acs.langmuir.3c02404 　

ISSN：0743-7463

eISSN：1520-5827
Structure of PSI-LHCI from Cyanidium caldarium provides evolutionary insights into conservation and diversity of red-lineage LHCs

Koji Kato, Tasuku Hamaguchi, Minoru Kumazawa, Yoshiki Nakajima, Kentaro Ifuku, Shunsuke Hirooka, Yuu Hirose, Shin-ya Miyagishima, Takehiro Suzuki, Keisuke Kawakami, Naoshi Dohmae, Koji Yonekura, Jian-Ren Shen, Ryo Nagao

BioRxiv　2023年10月27日
出版者・発行元： Cold Spring Harbor Laboratory
DOI： 10.1101/2023.10.25.563911 　

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Abstract Light-harvesting complexes (LHCs) are diversified among photosynthetic organisms, and their structural variety in photosystem I-LHC (PSI-LHCI) supercomplexes has been shown. However, structural and evolutionary correlations of red-lineage LHCs are unknown. Here we determined a 1.92-Å resolution cryo-electron microscopic structure of a PSI-LHCI supercomplex isolated from the red algaCyanidium caldariumRK-1 (NIES-2137) which is an important taxon in the Cyanidiophyceae, and subsequently investigated these correlations through structural comparisons and phylogenetic analysis. The PSI-LHCI structure shows five LHCI subunits together with a PSI-monomer core. The five LHCIs are composed of two Lhcr1s, two Lhcr2s, and one Lhcr3. Phylogenetic analysis of LHCs bound to PSI in red-lineage algae showed clear orthology of LHCs betweenC. caldariumandCyanidioschyzon merolae, whereas no orthologous relationships were found betweenC. caldariumLhcr1–3 and LHCs in other red-lineage PSI-LHCI structures. These findings provide evolutionary insights into conservation and diversity of red-lineage LHCs associated with PSI.
Enantioselectivity of discretized helical supramolecule consisting of achiral cobalt phthalocyanines via chiral-induced spin selectivity effect 査読有り

Hiroki Aizawa, Takuro Sato, Saori Maki-Yonekura, Koji Yonekura, Kiyofumi Takaba, Tasuku Hamaguchi, Taketoshi Minato, Hiroshi M. Yamamoto

Nature Communications　14　(1)　2023年7月28日
出版者・発行元： Springer Science and Business Media LLC
DOI： 10.1038/s41467-023-40133-z 　

eISSN：2041-1723

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Abstract Enantioselectivity of helical aggregation is conventionally directed either by its homochiral ingredients or by introduction of chiral catalysis. The fundamental question, then, is whether helical aggregation that consists only of achiral components can obtain enantioselectivity in the absence of chiral catalysis. Here, by exploiting enantiospecific interaction due to chiral-induced spin selectivity (CISS) that has been known to work to enantio-separate a racemic mixture of chiral molecules, we demonstrate the enantioselectivity in the assembly of mesoscale helical supramolecules consisting of achiral cobalt phthalocyanines. The helical nature in our supramolecules is revealed to be mesoscopically incorporated by dislocation-induced discretized twists, unlike the case of chiral molecules whose chirality are determined microscopically by chemical bond. The relevance of CISS effect in the discretized helical supramolecules is further confirmed by the appearance of spin-polarized current through the system. These observations mean that the application of CISS-based enantioselectivity is no longer limited to systems with microscopic chirality but is expanded to the one with mesoscopic chirality.
Measurement of charges and chemical bonding in a cryo-EM structure 査読有り

Saori Maki-Yonekura, Keisuke Kawakami, Kiyofumi Takaba, Tasuku Hamaguchi, Koji Yonekura

Communications Chemistry　6　(1)　98　2023年5月31日
出版者・発行元： Springer Science and Business Media LLC
DOI： 10.1038/s42004-023-00900-x 　

eISSN：2399-3669

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Abstract Hydrogen bonding, bond polarity, and charges in protein molecules play critical roles in the stabilization of protein structures, as well as affecting their functions such as enzymatic catalysis, electron transfer, and ligand binding. These effects can potentially be measured in Coulomb potentials using cryogenic electron microscopy (cryo-EM). We here present charges and bond properties of hydrogen in a sub-1.2 Å resolution structure of a protein complex, apoferritin, by single-particle cryo-EM. A weighted difference map reveals positive densities for most hydrogen atoms in the core region of the complex, while negative densities around acidic amino-acid side chains are likely related to negative charges. The former positive densities identify the amino- and oxo-termini of asparagine and glutamine side chains. The latter observations were verified by spatial-resolution selection and a dose-dependent frame series. The average position of the hydrogen densities depends on the parent bonded-atom type, and this is validated by the estimated level of the standard uncertainties in the bond lengths.
Structural resolution of a small organic molecule by serial X-ray free-electron laser and electron crystallography 査読有り

Kiyofumi Takaba, Saori Maki-Yonekura, Ichiro Inoue, Kensuke Tono, Tasuku Hamaguchi, Keisuke Kawakami, Hisashi Naitow, Tetsuya Ishikawa, Makina Yabashi, Koji Yonekura

Nature Chemistry　2023年3月20日
出版者・発行元： Springer Science and Business Media LLC
DOI： 10.1038/s41557-023-01162-9 　

ISSN：1755-4330

eISSN：1755-4349
Unnaturally Distorted Hexagonal Protein Ring Alternatingly Reorganized from Two Distinct Chemically Modified Proteins 査読有り

Tomoki Himiyama, Tasuku Hamaguchi, Koji Yonekura, Tsutomu Nakamura

Bioconjugate Chemistry　2023年3月8日
出版者・発行元： American Chemical Society (ACS)
DOI： 10.1021/acs.bioconjchem.3c00057 　

ISSN：1043-1802

eISSN：1520-4812
Structure of a monomeric photosystem I core associated with iron-stress-induced-A proteins from Anabaena sp. PCC 7120. 国際誌査読有り

Ryo Nagao, Koji Kato, Tasuku Hamaguchi, Yoshifumi Ueno, Naoki Tsuboshita, Shota Shimizu, Miyu Furutani, Shigeki Ehira, Yoshiki Nakajima, Keisuke Kawakami, Takehiro Suzuki, Naoshi Dohmae, Seiji Akimoto, Koji Yonekura, Jian-Ren Shen

Nature communications　14　(1)　920-920　2023年2月17日

DOI： 10.1038/s41467-023-36504-1 　

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Iron-stress-induced-A proteins (IsiAs) are expressed in cyanobacteria under iron-deficient conditions. The cyanobacterium Anabaena sp. PCC 7120 has four isiA genes; however, their binding property and functional roles in PSI are still missing. We analyzed a cryo-electron microscopy structure of a PSI-IsiA supercomplex isolated from Anabaena grown under an iron-deficient condition. The PSI-IsiA structure contains six IsiA subunits associated with the PsaA side of a PSI core monomer. Three of the six IsiA subunits were identified as IsiA1 and IsiA2. The PSI-IsiA structure lacks a PsaL subunit; instead, a C-terminal domain of IsiA2 occupies the position of PsaL, which inhibits the oligomerization of PSI, leading to the formation of a PSI monomer. Furthermore, excitation-energy transfer from IsiAs to PSI appeared with a time constant of 55 ps. These findings provide insights into both the molecular assembly of the Anabaena IsiA family and the functional roles of IsiAs.
Structure and Function of Gli123 Involved in Mycoplasma mobile Gliding 査読有り

Daiki Matsuike, Yuhei O. Tahara, Takahiro Nonaka, Heng Ning Wu, Tasuku Hamaguchi, Hisashi Kudo, Yuuki Hayashi, Munehito Arai, Makoto Miyata

Journal of Bacteriology　2023年2月7日
出版者・発行元： American Society for Microbiology
DOI： 10.1128/jb.00340-22 　

ISSN：0021-9193

eISSN：1098-5530

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Mycoplasmas are pathogenic bacteria that are widespread in animals. They are characterized by small cell and genome sizes but are equipped with unique abilities for infection, such as surface variation and gliding.
Core and rod structures of a thermophilic cyanobacterial light-harvesting phycobilisome 査読有り

Keisuke Kawakami, Tasuku Hamaguchi, Yuu Hirose, Daisuke Kosumi, Makoto Miyata, Nobuo Kamiya, Koji Yonekura

Nature Communications　13　(1)　2022年6月
出版者・発行元： Springer Science and Business Media LLC
DOI： 10.1038/s41467-022-30962-9 　

eISSN：2041-1723

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Abstract Cyanobacteria, glaucophytes, and rhodophytes utilize giant, light-harvesting phycobilisomes (PBSs) for capturing solar energy and conveying it to photosynthetic reaction centers. PBSs are compositionally and structurally diverse, and exceedingly complex, all of which pose a challenge for a comprehensive understanding of their function. To date, three detailed architectures of PBSs by cryo-electron microscopy (cryo-EM) have been described: a hemiellipsoidal type, a block-type from rhodophytes, and a cyanobacterial hemidiscoidal-type. Here, we report cryo-EM structures of a pentacylindrical allophycocyanin core and phycocyanin-containing rod of a thermophilic cyanobacterial hemidiscoidal PBS. The structures define the spatial arrangement of protein subunits and chromophores, crucial for deciphering the energy transfer mechanism. They reveal how the pentacylindrical core is formed, identify key interactions between linker proteins and the bilin chromophores, and indicate pathways for unidirectional energy transfer.
Theoretical Model of the Far-Red-Light-Adapted Photosystem I Reaction Center of Cyanobacterium Acaryochloris marina Using Chlorophyll d and the Effect of Chlorophyll Exchange 査読有り

Akihiro Kimura, Hirotaka Kitoh-Nishioka, Toshimichi Aota, Tasuku Hamaguchi, Koji Yonekura, Keisuke Kawakami, Kyoko Shinzawa-Itoh, Natsuko Inoue-Kashino, Kentaro Ifuku, Eiki Yamashita, Yasuhiro Kashino, Shigeru Itoh

The Journal of Physical Chemistry B　2022年5月26日
出版者・発行元： American Chemical Society (ACS)
DOI： 10.1021/acs.jpcb.2c00869 　

ISSN：1520-6106

eISSN：1520-5207
Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus 国際誌査読有り

Koji Kato, Tasuku Hamaguchi, Ryo Nagao, Keisuke Kawakami, Yoshifumi Ueno, Takehiro Suzuki, Hiroko Uchida, Akio Murakami, Yoshiki Nakajima, Makio Yokono, Seiji Akimoto, Naoshi Dohmae, Koji Yonekura, Jian-Ren Shen

eLife　11　2022年4月11日
出版者・発行元： eLife Sciences Publications, Ltd
DOI： 10.7554/elife.73990 　

eISSN：2050-084X

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Photosystem I (PSI) is a multi-subunit pigment-protein complex that functions in light-harvesting and photochemical charge-separation reactions, followed by reduction of NADP to NADPH required for CO₂ fixation in photosynthetic organisms. PSI from different photosynthetic organisms has a variety of chlorophylls (Chls), some of which are at lower-energy levels than its reaction center P700, a special pair of Chls, and are called low-energy Chls. However, the sites of low-energy Chls are still under debate. Here, we solved a 2.04-Å resolution structure of a PSI trimer by cryo-electron microscopy from a primordial cyanobacterium Gloeobacter violaceus PCC 7421, which has no low-energy Chls. The structure shows the absence of some subunits commonly found in other cyanobacteria, confirming the primordial nature of this cyanobacterium. Comparison with the known structures of PSI from other cyanobacteria and eukaryotic organisms reveals that one dimeric and one trimeric Chls are lacking in the Gloeobacter PSI. The dimeric and trimeric Chls are named Low1 and Low2, respectively. Low2 is missing in some cyanobacterial and eukaryotic PSIs, whereas Low1 is absent only in Gloeobacter. These findings provide insights into not only the identity of low-energy Chls in PSI, but also the evolutionary changes of low-energy Chls in oxyphototrophs.
Hydrogen properties and charges in a sub-1.2 Å resolution cryo-EM structure revealed by a cold field emission beam

Saori Maki-Yonekura, Keisuke Kawakami, Tasuku Hamaguchi, Kiyofumi Takaba, Koji Yonekura

2021年12月22日
出版者・発行元： Cold Spring Harbor Laboratory
DOI： 10.1101/2021.12.21.473430 　

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Abstract The cold field emission (CFE) beam produces the less-attenuated contrast transfer function of electron microscopy, thereby enhancing high-resolution signals and this particularly benefits higher-resolution single particle cryogenic electron microscopy. Here, we present a sub-1.2 Å resolution structure of a standard protein sample, apoferritin. Image data were collected with the CFE beam in a high-throughput scheme while minimizing beam tilt deviations from the coma-free axis. A difference map reveals positive densities for most hydrogen atoms in the core region of the protein complex including those in water molecules, while negative densities around acidic amino-acid side chains likely represent negative charges. The position of the hydrogen densities depends on parent bonded-atom type, which is validated by an estimated level of coordinate errors.
Machine learning-based real-time object locator/evaluator for cryo-EM data collection 国際誌査読有り

Koji Yonekura, Saori Maki-Yonekura, Hisashi Naitow, Tasuku Hamaguchi, Kiyofumi Takaba

Communications Biology　4　(1)　1044-1044　2021年12月
出版者・発行元： Springer Science and Business Media LLC
DOI： 10.1038/s42003-021-02577-1 　

eISSN：2399-3642

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<title>Abstract</title>In cryo-electron microscopy (cryo-EM) data collection, locating a target object is error-prone. Here, we present a machine learning-based approach with a real-time object locator named yoneoLocr using YOLO, a well-known object detection system. Implementation shows its effectiveness in rapidly and precisely locating carbon holes in single particle cryo-EM and in locating crystals and evaluating electron diffraction (ED) patterns in automated cryo-electron crystallography (cryo-EX) data collection. The proposed approach will advance high-throughput and accurate data collection of images and diffraction patterns with minimal human operation.
Hydrogen properties in an organic molecule revealed by XFEL and electron crystallography

Kiyofumi Takaba, Saori Maki-Yonekura, Ichiro Inoue, Kensuke Tono, Tasuku Hamaguchi, Keisuke Kawakami, Hisahi Naitow, Tetsuya Ishikawa, Makina Yabashi, Koji Yonekura

2021年11月9日
出版者・発行元： American Chemical Society (ACS)
DOI： 10.26434/chemrxiv-2021-jvbfl 　

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Structure analysis of small crystals is important in synthetic organic chemistry, pharmaceutical and material sciences, and related areas, as the conformation of these molecules may differ in large and small crystals, thus affecting the interpretation of their functional properties and drug efficacy. From small crystals, X-ray and electron beams could furnish electron densities and Coulomb potentials of target molecules, respectively. The two beams provide distinctly different information, and this potential has not been fully explored. Here we present the detailed structure of an organic molecule, rhodamine-6g by X-ray free-electron laser (XFEL) and electron crystallography from the same sample batch of microcrystals. This is the first organic molecular structure determined using XFEL at subatomic resolution. Direct comparison between the electron-density and the Coulomb-potential maps together with theoretical models based on Poisson’s equation shows that the position of hydrogen atoms depends on bond type and charge distribution. The combined approach could lead to better insights into their chemical and/or binding properties for a broad range of organic molecules.
Structural basis for the absence of low-energy chlorophylls responsible for photoprotection from a primitive cyanobacterial PSI

Koji Kato, Tasuku Hamaguchi, Ryo Nagao, Keisuke Kawakami, Yoshifumi Ueno, Takehiro Suzuki, Hiroko Uchida, Akio Murakami, Yoshiki Nakajima, Makio Yokono, Seiji Akimoto, Naoshi Dohmae, Koji Yonekura, Jian-Ren Shen

2021年10月1日
出版者・発行元： Cold Spring Harbor Laboratory
DOI： 10.1101/2021.09.29.462462 　

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<title>Abstract</title>Photosystem I (PSI) of photosynthetic organisms is a multi-subunit pigment-protein complex and functions in light harvesting and photochemical charge-separation reactions, followed by reduction of NADP to NADPH required for CO₂ fixation. PSI from different photosynthetic organisms has a variety of chlorophylls (Chls), some of which are at lower-energy levels than its reaction center P700, a special pair of Chls, and are called low-energy Chls. However, the site of low-energy Chls is still under debate. Here, we solved a 2.04-Å resolution structure of a PSI trimer by cryo-electron microscopy from a primitive cyanobacterium <italic>Gloeobacter violaceus</italic> PCC 7421, which has no low-energy Chls. The structure showed absence of some subunits commonly found in other cyanobacteria, confirming the primitive nature of this cyanobacterium. Comparison with the known structures of PSI from other cyanobacteria and eukaryotic organisms reveals that one dimeric and one trimeric Chls are lacking in the <italic>Gloeobacter</italic> PSI. The dimeric and trimeric Chls are named Low1 and Low2, respectively. Low2 does not exist in some cyanobacterial and eukaryotic PSIs, whereas Low1 is absent only in <italic>Gloeobacter</italic>. Since <italic>Gloeobacter</italic> is susceptible to light, this indicates that Low1 serves as a main photoprotection site in most oxyphototrophs, whereas Low2 is involved in either energy transfer or energy quenching in some of the oxyphototrophs. Thus, these findings provide insights into not only the functional significance of low-energy Chls in PSI, but also the evolutionary changes of low-energy Chls responsible for the photoprotection machinery from photosynthetic prokaryotes to eukaryotes.
Complementary use of high-resolution and high-precision cryo-ED and EM

Koji Yonekura, Saori Maki-Yonekura, Kiyofumi Takaba, Tasuku Hamaguchi, Hisashi Naitow, Keisuke Kawakami

Microscopy and Microanalysis　27　(S1)　204-206　2021年8月
出版者・発行元： Cambridge University Press (CUP)
DOI： 10.1017/s143192762100132x 　

ISSN：1431-9276

eISSN：1435-8115
Chained Structure of Dimeric F1-like ATPase in Mycoplasma mobile Gliding Machinery 国際誌査読有り

Takuma Toyonaga, Takayuki Kato, Akihiro Kawamoto, Noriyuki Kodera, Tasuku Hamaguchi, Yuhei O. Tahara, Toshio Ando, Keiichi Namba, Makoto Miyata

mBio　e0141421　2021年7月20日
出版者・発行元： American Society for Microbiology
DOI： 10.1128/mbio.01414-21 　

eISSN：2150-7511

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F ₁ F _o -ATPase, a rotary ATPase, is widespread in the membranes of mitochondria, chloroplasts, and bacteria and converts ATP energy with a proton motive force across the membrane by its physical rotation. Homologous protein complexes play roles in ion and protein transport. <named-content content-type="genus-species">Mycoplasma mobile</named-content> , a pathogenic bacterium, was recently suggested to have a special motility system evolutionarily derived from F ₁ -ATPase.
Cryo-EM structure of monomeric photosystem II at 2.78 Å resolution reveals factors important for the formation of dimer 国際誌査読有り

Huaxin Yu, Tasuku Hamaguchi, Yoshiki Nakajima, Koji Kato, Keisuke Kawakami, Fusamichi Akita, Koji Yonekura, Jian-Ren Shen

Biochimica et Biophysica Acta (BBA) - Bioenergetics　1862　(10)　148471-148471　2021年7月
出版者・発行元： Elsevier BV
DOI： 10.1016/j.bbabio.2021.148471 　

ISSN：0005-2728

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Photosystem II (PSII) functions mainly as a dimer to catalyze the light energy conversion and water oxidation reactions. However, monomeric PSII also exists and functions in vivo in some cases. The crystal structure of monomeric PSII has been solved at 3.6 Å resolution, but it is still not clear which factors contribute to the formation of the dimer. Here, we solved the structure of PSII monomer at a resolution of 2.78 Å using cryo-electron microscopy (cryo-EM). From our cryo-EM density map, we observed apparent differences in pigments and lipids in the monomer-monomer interface between the PSII monomer and dimer. One β-carotene and two sulfoquinovosyl diacylglycerol (SQDG) molecules are found in the monomer-monomer interface of the dimer structure but not in the present monomer structure, although some SQDG and other lipid molecules are found in the analogous region of the low-resolution crystal structure of the monomer, or cryo-EM structure of an apo-PSII monomer lacking the extrinsic proteins from Synechocystis sp. PCC 6803. In the current monomer structure, a large part of the PsbO subunit was also found to be disordered. These results indicate the importance of the β-carotene, SQDG and PsbO in formation of the PSII dimer.
Structural implications for a phycobilisome complex from the thermophilic cyanobacterium Thermosynechococcus vulcanus 査読有り

Keisuke Kawakami, Ryo Nagao, Yuhei O. Tahara, Tasuku Hamaguchi, Takehiro Suzuki, Naoshi Dohmae, Daisuke Kosumi, Jian-Ren Shen, Makoto Miyata, Koji Yonekura, Nobuo Kamiya

Biochimica et Biophysica Acta (BBA) - Bioenergetics　1862　(9)　148458-148458　2021年5月
出版者・発行元： Elsevier BV
DOI： 10.1016/j.bbabio.2021.148458 　

ISSN：0005-2728
Structural insights into the targeting specificity of ubiquitin ligase for S.cerevisiae isocitrate lyase but not C.albicans isocitrate lyase 査読有り

Keito Hiragi, Kazuya Nishio, Shu Moriyama, Tasuku Hamaguchi, Akira Mizoguchi, Koji Yonekura, Kazutoshi Tani, Tsunehiro Mizushima

Journal of Structural Biology　107748-107748　2021年5月
出版者・発行元： Elsevier BV
DOI： 10.1016/j.jsb.2021.107748 　

ISSN：1047-8477
Real-time object locator for cryo-EM data collection --- You only navigate EM once ---

Koji Yonekura, Saori Maki-Yonekura, Hisashi Naitow, Tasuku Hamaguchi, Kiyofumi Takaba

2021年4月9日

DOI： 10.1101/2021.04.07.438905 　
Structure of the far-red light utilizing photosystem I of Acaryochloris marina 国際誌査読有り

Tasuku Hamaguchi, Keisuke Kawakami, Kyoko Shinzawa-Itoh, Natsuko Inoue-Kashino, Shigeru Itoh, Kentaro Ifuku, Eiki Yamashita, Kou Maeda, Koji Yonekura, Yasuhiro Kashino

Nature Communications　12　(1)　2333-2333　2021年4月
出版者・発行元： Springer Science and Business Media LLC
DOI： 10.1038/s41467-021-22502-8 　

eISSN：2041-1723

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<title>Abstract</title><italic>Acaryochloris marina</italic> is one of the cyanobacterial species that can use far-red light to drive photochemical reactions for oxygenic photosynthesis. Here, we report the structure of <italic>A. marina</italic> photosystem I (PSI) reaction center, determined by cryo-electron microscopy at 2.58 Å resolution. The structure reveals an arrangement of electron carriers and light-harvesting pigments distinct from other type I reaction centers. The paired chlorophyll, or special pair (also referred to as P740 in this case), is a dimer of chlorophyll <italic>d</italic> and its epimer chlorophyll <italic>d</italic>′. The primary electron acceptor is pheophytin <italic>a</italic>, a metal-less chlorin. We show the architecture of this PSI reaction center is composed of 11 subunits and we identify key components that help explain how the low energy yield from far-red light is efficiently utilized for driving oxygenic photosynthesis.
Advances in cryo-EM and ED with a cold-field emission beam and energy filtration —Refinements of the CRYO ARM 300 system in RIKEN SPring-8 center— 国際誌査読有り

Saori Maki-Yonekura, Tasuku Hamaguchi, Hisashi Naitow, Kiyofumi Takaba, Koji Yonekura

Microscopy　70　(2)　232-240　2021年3月24日
出版者・発行元： Oxford University Press (OUP)
DOI： 10.1093/jmicro/dfaa052 　

ISSN：2050-5698

eISSN：2050-5701

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<title>Abstract</title> We have designed and evaluated a cryo-electron microscopy (cryo-EM) system for higher-resolution single particle analysis and high-precision electron 3D crystallography. The system comprises a JEOL CRYO ARM 300 electron microscope—the first machine of this model—and a direct detection device camera, a scintillator-coupled camera, GPU clusters connected with a camera control computer and software for automated-data collection and efficient and accurate operation. The microscope provides parallel illumination of a highly coherent 300-kV electron beam to a sample from a cold-field emission gun and filters out energy-loss electrons through the sample with an in-column energy filter. The gun and filter are highly effective in improving imaging and diffraction, respectively, and have provided high quality data since July 2018. We here report on the characteristics of the cryo-EM system, updates, our progress and future plan for running such cryo-EM machines in RIKEN SPring-8 Center.
High-resolution cryo-EM structure of photosystem II reveals damage from high-dose electron beams 国際誌査読有り

Koji Kato, Naoyuki Miyazaki, Tasuku Hamaguchi, Yoshiki Nakajima, Fusamichi Akita, Koji Yonekura, Jian-Ren Shen

Communications Biology　4　(1)　382-382　2021年3月
出版者・発行元： Springer Science and Business Media LLC
DOI： 10.1038/s42003-021-01919-3 　

eISSN：2399-3642

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<title>Abstract</title>Photosystem II (PSII) plays a key role in water-splitting and oxygen evolution. X-ray crystallography has revealed its atomic structure and some intermediate structures. However, these structures are in the crystalline state and its final state structure has not been solved. Here we analyzed the structure of PSII in solution at 1.95 Å resolution by single-particle cryo-electron microscopy (cryo-EM). The structure obtained is similar to the crystal structure, but a PsbY subunit was visible in the cryo-EM structure, indicating that it represents its physiological state more closely. Electron beam damage was observed at a high-dose in the regions that were easily affected by redox states, and reducing the beam dosage by reducing frames from 50 to 2 yielded a similar resolution but reduced the damage remarkably. This study will serve as a good indicator for determining damage-free cryo-EM structures of not only PSII but also all biological samples, especially redox-active metalloproteins.
Cryo-EM and ED with a Cold-Field Emission Beam and Energy Filtration 査読有り

Koji Yonekura, Saori Maki-Yonekura, Tasuku Hamaguchi, Hisashi Naitow, Kiyofumi Takaba, Keisuke Kawakami

Applications of Microscopy in Materials and Life Sciences　233-241　2021年
出版者・発行元： Springer Singapore
DOI： 10.1007/978-981-16-2982-2_23 　

ISSN：2662-3161

eISSN：2662-317X
High-resolution cryo-EM structure of photosystem II: Effects of electron beam damage

Koji Kato, Naoyuki Miyazaki, Tasuku Hamaguchi, Yoshiki Nakajima, Fusamichi Akita, Koji Yonekura, Jian-Ren Shen

2020年10月19日
出版者・発行元： Cold Spring Harbor Laboratory
DOI： 10.1101/2020.10.18.344648 　

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<jats:title>Abstract</jats:title><jats:p>Photosystem II (PSII) plays a key role in water-splitting and oxygen evolution. X-ray crystallography has revealed its atomic structure and some intermediate structures. However, these structures are in the crystalline state, and its final state structure has not been solved because of the low efficiencies of the S-state transitions in the crystals. Here we analyzed the structure of PSII in solution at 1.95 Å resolution by single-particle cryo-electron microscopy (cryo-EM). The structure obtained is similar to the crystal structure, but a PsbY subunit was visible in the cryo-EM structure, indicating that it represents its physiological state more closely. Electron beam damage was observed at a high-dose in the regions that were easily affected by redox states, which was reduced by reducing the electron dose. This study will serve as a good indicator for determining damage-free cryo-EM structures of not only PSII but also all biological samples, especially redox-active metalloproteins.</jats:p>
Erratum to "A new cryo-EM system for single particle analysis" [J. Struct. Biol. 207 (1) (2019) 40-48]. 国際誌

Tasuku Hamaguchi, Saori Maki-Yonekura, Hisashi Naitow, Yoshinori Matsuura, Tetsuya Ishikawa, Koji Yonekura

Journal of structural biology　211　(3)　107558-107558　2020年9月1日

DOI： 10.1016/j.jsb.2020.107558 　
Apple latent spherical virus structure with stable capsid frame supports quasi-stable protrusions expediting genome release 査読有り

Hisashi Naitow, Tasuku Hamaguchi, Saori Maki-Yonekura, Masamichi Isogai, Nobuyuki Yoshikawa, Koji Yonekura

Communications Biology　3　(1)　2020年9月
出版者・発行元： Springer Science and Business Media LLC
DOI： 10.1038/s42003-020-01217-4 　

eISSN：2399-3642
ATP合成酵素とPGKから進化したMycoplasma mobile滑走モーターの構造

豊永拓真, 加藤貴之, 川本晃大, 浜口祐, 古寺哲幸, 安藤敏夫, 難波啓一, 宮田真人

日本マイコプラズマ学会雑誌　(46)　44-46　2020年3月
出版者・発行元：日本マイコプラズマ学会
ISSN：1340-2382
Tidy up cryo-EM sample grids with 3D printed tools 国際誌査読有り

Tasuku Hamaguchi, Koji Yonekura

Journal of Structural Biology　209　(1)　107414-107414　2020年1月
出版者・発行元： Elsevier BV
DOI： 10.1016/j.jsb.2019.107414 　

ISSN：1047-8477

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Cryo-EM technology has developed to the point of high-throughput structure determination of biological macromolecules embedded in vitreous ice. Nonetheless, challenging targets need extensive sample screening, often of many cryo-EM sample grids prepared under various conditions. We have designed and made tools for manipulating sample grids in storage cases. These tools are made of a plastic fiber using a wide-use 3D printer, a fused deposition modeling type, and polished under acetone gas. A grid case stacker organizes many frozen-hydrated cryo-EM grids and the stackers can be piled up inside a standard 50 mL centrifuge tube. We have also introduced tools that facilitate handling of grid cases under liquid nitrogen and a stocker of the grid retainers contained in a CRYO ARM electron microscope. Blueprints of the tools named CryoGridTools are available from a GitHub site.
A new cryo-EM system for single particle analysis 国際誌査読有り

Tasuku Hamaguchi, Saori Maki-Yonekura, Hisashi Naitow, Yoshinori Matsuura, Tetsuya Ishikawa, Koji Yonekura

Journal of Structural Biology　207　(1)　40-48　2019年7月
出版者・発行元： Elsevier BV
DOI： 10.1016/j.jsb.2019.04.011 　

ISSN：1047-8477

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A new cryo-EM system has been investigated for single particle analysis of protein structures. The system provides parallel illumination of a highly-coherent 300 kV electron beam from a cold-field emission gun, and boosts image contrast with an in-column energy filter and a hole-free phase plate. It includes motorized cryo-sample loading and automated liquid-nitrogen filling for cooling multiple samples. In this study, we describe gun and electron beam characteristics, and demonstrate the suitability of this system for single particle reconstructions. The performance of the system is tested on two examples, a spherical virus and apoferritin. GUI programs have also been developed to control and monitor the system for correct illumination, imaging with less ellipticity and steady magnification, and timing of flashing and liquid-nitrogen filling. These programs are especially useful for efficient application of the system to single particle cryo-EM.
Identification of novel protein domain for sialyloligosaccharide binding essential to Mycoplasma mobile gliding. 国際誌査読有り

Hamaguchi T, Kawakami M, Furukawa H, Miyata M

FEMS Microbiology Letters　366　(3)　fnz016　2019年1月21日

DOI： 10.1093/femsle/fnz016 　
Integrated Information and Prospects for Gliding Mechanism of the Pathogenic Bacterium Mycoplasma pneumoniae 査読有り

Makoto Miyata, Tasuku Hamaguchi

FRONTIERS IN MICROBIOLOGY　7　960　2016年6月

DOI： 10.3389/fmicb.2016.00960 　

ISSN：1664-302X
Prospects for the gliding mechanism of Mycoplasma mobile 査読有り

Makoto Miyata, Tasuku Hamaguchi

CURRENT OPINION IN MICROBIOLOGY　29　15-21　2016年2月

DOI： 10.1016/j.mib.2015.08.010 　

ISSN：1369-5274

eISSN：1879-0364
C3-P-08Structure and function of P1 adhesin ofMycoplasma pneumoniae

U Matsumoto, Yoshito Kawakita, Tsuyoshi Kenri, Shigetaro Mori, Tasuku Hamaguchi, Miki Kinoshita, Akihiro Kawamoto, Takayuki Kato, Keiichi Namba, Makoto Miyata

Microscopy　64　(suppl 1)　i130.1-i130　2015年11月
出版者・発行元： Oxford University Press ({OUP})
DOI： 10.1093/jmicro/dfv311 　

ISSN：2050-5698
C3-P-09Structural analyses of Gli123 protein, essential forMycoplasma mobilegliding

Daiki Matsuike, Yuhei O Tahara, Tasuku Hamaguchi, Makoto Miyata

Microscopy　64　(suppl 1)　i130.2-i130　2015年11月
出版者・発行元： Oxford University Press ({OUP})
DOI： 10.1093/jmicro/dfv312 　

ISSN：2050-5698
Gliding Motility of Mycoplasma mobile on Uniform Oligosaccharides 査読有り

Taishi Kasai, Tasuku Hamaguchi, Makoto Miyata

JOURNAL OF BACTERIOLOGY　197　(18)　2952-2957　2015年9月

DOI： 10.1128/JB.00335-15 　

ISSN：0021-9193

eISSN：1098-5530
Reprint of “Prospects for the gliding mechanism of Mycoplasma mobile”

Miyata, M., Hamaguchi, T.

Current Opinion in Microbiology　28　2015年

DOI： 10.1016/j.mib.2015.12.002 　

ISSN：1879-0364 1369-5274
Reprint of “Prospects for the gliding mechanism of Mycoplasma mobile”

Makoto Miyata, Tasuku Hamaguchi

Current Opinion in Microbiology　28　122-128　2015年
出版者・発行元： Elsevier {BV}
DOI： 10.1016/j.mib.2015.12.002 　

ISSN：1369-5274
Purification, characterization and molecular cloning of a novel endo-beta-N-acetylglucosaminidase from the basidiomycete, Flammulina velutipes 査読有り

Tasuku Hamaguchi, Tsukasa Ito, Yukako Inoue, Tipaporn Limpaseni, Piamsook Pongsawasdi, Kazuo Ito

GLYCOBIOLOGY　20　(4)　420-432　2010年4月

DOI： 10.1093/glycob/cwp188 　

ISSN：0959-6658

eISSN：1460-2423
エンド-β-N-アセチルグルコサミニダーゼHSによる糖タンパク質からのアスパラギン結合コンプレックス型糖鎖の転移導入査読有り

宮川貴美子, 松本睦美, 藪野重毅, 河上直子, 濱口祐, 飯塚勝, 南浦能至, 伊藤和央

Journal of applied glycoscience　54　(2)　139-146　2007年
出版者・発行元： The Japanese Society of Applied Glycoscience
DOI： 10.5458/jag.54.139 　

ISSN：1344-7882

eISSN：1880-7291

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エンド-β-N-アセチルグルコサミニダーゼは，アスパラギン結合型糖鎖のキトビオース間を適当な水酸基結合分子によって分解し，糖鎖をこの分子に転移する．われわれが発見した酵素 (エンドHS) は，糖タンパク質から，2，3，4本鎖コンプレックス型糖鎖を容易に遊離させる唯一の酵素で，われわれはエンドHSの糖鎖転移特性を検討してきた．エンドHSはヒトトランスフェリンから2本鎖コンプレックス型糖鎖を転移し，生成物は受容体濃度依存的に増加した．このとき，PNP-α/β-D-Glc，PNP-α/β-D-Gal，PNP-β-D-Man，PNP-β-D-Xyl，PNP-β-D-GlcNAcへ糖鎖を転移し，α/β-アノマーを区別しなかった．他の酵素は，糖の4位の水酸基がエカトリアルであることを要求するためGalには転移しない．したがって，エンドHSは，受容体分子の水酸基の立体配置認識が他の酵素とは異なっていた．生成した転移生成物は反応液中でほとんど減少せず，転移した糖鎖は，GlcNAcβ1-4以外の様式でGlcと結合しているか，エンドHSは糖鎖構造中のGlcNAc-GlcNAc間は加水分解するが転移生成物中のGlcNAc-Glc間は加水分解しにくいものと考えられた．また，エンドHSはPNP-グリセロールへも糖鎖を転移し，糖鎖供与体に対するK_m値は，受容体がPNP-β-D-Glcの場合と大差はなく，エンドHSの糖鎖供与体に対する親和性は，受容体分子の構造の違いによる影響を受けにくいものと考えられた．さらに，本酵素は糖タンパク質から3および4本鎖コンプレックス型糖鎖を転移した．また，糖ペプチドからも糖鎖を転移した．一方，糖アスパラギンからも2および3本鎖コンプレックス型糖鎖を各種単糖，オリゴ糖，糖アルコールおよび配糖体に転移した．また，極性有機溶媒が転移効率に有効であった．エンドHSによって，糖タンパク質由来のさまざまなコンプレックス型糖鎖をさまざまな受容体分子に直接導入し，糖鎖と受容体分子双方の機能を持つ機能性糖鎖ハイブリッド創成の実現の道が開いた．
Evidence for the transglycosylation of complex type oligosaccharides of glycoproteins by endo-beta-N-acetylglucosaminidase HS 査読有り

Kazuo Ito, Kimiko Miyagawa, Mutsumi Matsumoto, Shigeki Yabuno, Naoko Kawakami, Tasuku Hamaguchi, Masaru Iizuka, Noshi Minamiura

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS　454　(1)　89-99　2006年10月

DOI： 10.1016/j.abb.2006.06.004 　

ISSN：0003-9861

︎全件表示 ︎最初の5件までを表示

MISC 2

クロロフィルdを持つ遠赤色光型反応中心A.marina PSIの光捕集機構に関する理論解析:クロロフィルa-型PSIとの比較

木村明洋, 鬼頭宏任, 青田俊道, 浜口祐, 米倉功治, 川上恵典, 新沢(伊藤)恭子, 井上(菓子野)名津子, 伊福健太郎, 菓子野康浩, 山下栄樹, 伊藤繁

日本物理学会講演概要集(CD-ROM)　77　(1)　2022年

ISSN： 2189-079X
汎用3Dプリンターを用いた発光模型査読有り

浜口祐, 川上勝, 宮田真人

一般社団法人日本生物物理学会生物物理　57　(4)　216-218　2017年
出版者・発行元：一般社団法人日本生物物理学会
DOI： 10.2142/biophys.57.216

講演・口頭発表等 39

低GC生物マイコプラズマ由来新規Cas9の探索

上野莉香子, 池内健, 豊永拓真, 濵口祐, 米倉功治

公益社団法人日本顕微鏡学会第81回学術講演会　2025年6月11日
クライオEELS/EF-TEMによる凍結溶媒内バイオマテリアルの多元素マッピング観察

海原大輔, 佐藤庸平, 濵口祐, 米倉功治

公益社団法人日本顕微鏡学会第81回学術講演会　2025年6月10日
CryoEMによって可視化したマイコプラズマ滑走型Rotary ATPaseの回転

豊永拓真, 海原大輔, 濵口祐, 米倉功治

公益社団法人日本顕微鏡学会第81回学術講演会　2025年6月9日
Cryo-EM Analysis of Chained G1-ATPase, Motor for Mycoplasma Gliding 国際会議

Takuma Toyonaga, Daisuke Unabara, Tasuku Hamaguchi, Makoto Miyata, Koji Yonekura

Sixth Japan-Canada Microscopy Societies Joint Symposium 2025　2025年6月10日
Cryo-EM Structure of PSI-LHCI from a Red alga Cyanidium caldarium 国際会議

Koji Kato, Tasuku Hamaguchi, Minoru Kumazawa, Yoshiki Nakajima, Kentaro Ifuku, Yuu Hirose, Keisuke Kawakami, Koji Yonekura, Ryo Nagao, Jian-Ren Shen

The 13th Asia Pacific Microscopy Congress 2025 (APMC13)　2025年2月4日
東北大・多元研の取り組み

濵口祐

第3回クライオ電子顕微鏡施設技術交流会　2024年12月18日
マイコプラズマ滑走運動を駆動する新奇回転分子モーターのCryoEM構造

豊永拓真, 濵口祐, 宮田真人, 米倉功治

第24回東北大学多元物質科学研究所研究発表会　2024年12月12日
クライオFIB-SEMおよびクライオTEMを利用した納豆芽胞の可視化

丹羽瑠美, 濵口祐, 米倉功治

第24回東北大学多元物質科学研究所研究発表会　2024年12月12日
クライオEELS/EF-TEMによる凍結溶媒内ソフトマテリアルの元素マッピング観察

海原大輔, 佐藤庸平, 濵口祐, 米倉功治

第24回東北大学多元物質科学研究所研究発表会　2024年12月12日
Structure of the far-red light utilizing photosystem I of Acaryochloris marina 国際会議

Keisuke Kawakami, Tasuku Hamaguchi, Kyoko Shinzawa-Itoh, Natsuko Inoue-Kashino, Shigeru Itoh, Kentaro Ifuku, Eiki Yamashita, Kou Maeda, Koji Yonekura, Yasuhiro, Kashino

2nd Asia-Oceania International Congress on Photosynthesis (AOICP)　2024年9月18日
Cryo-EM structure of PSI-LHCI from a red alga Cyanidium caldarium 国際会議

Koji Kato, Tasuku Hamaguchi, Minoru Kumazawa, Yoshiki Nakajima, Kentaro Ifuku, Yuu Hirose, Keisuke Kawakami, Koji Yonekura, Ryo Nagao, Jian-Ren Shen

2nd Asia-Oceania International Congress on Photosynthesis (AOICP)　2024年9月18日
Cryo-EM Observations and Analyses in Life/material Science 招待有り

濵口祐

令和6年度化学系学協会東北大会　2024年9月14日
クライオ電子顕微鏡によるソフトマテリアル局所構造の可視化に向けたアプローチとその成果招待有り

濵口祐

日本顕微鏡学会ソフトマテリアル分科会 2024 年度第 1 回講演会～ソフトマテリアル向けの最新局所構造解析　2024年7月25日
CryoEM structure of dimeric F1-like ATPase in Mycoplasma mobile suggests a rotary catalytic mechanism for the gliding motility 国際会議

Takuma TOYONAGA, Takayuki KATO, Akihiro KAWAMOTO, Tomoko MIYATA, Keisuke KAWAKAMI, Junso FUJITA, Tasuku HAMAGUCHI, Keiichi NAMBA, Makoto MIYATA

21st IUPAB Congress 2024　2024年6月28日
クライオEELS/EF-TEMによる凍結溶媒内ソフトマテリアルの元素マッピング観察

海原大輔, 佐藤庸平, 濵口祐, 米倉功治

日本顕微鏡学会第80回学術講演会　2024年6月4日
溶液中の粒子配向を改善した高精度単粒子解析

岡圭吾, 濵口祐, 海原大輔, 米倉功治

日本顕微鏡学会第80回学術講演会　2024年6月3日
クライオ電子顕微鏡によるオイルワックスゲルの新たな評価手法の検討

太田裕基, 山下美香, 鈴木留佳, 畑毅, 濵口祐, 陣内浩司

日本顕微鏡学会第80回学術講演会　2024年6月3日
クライオ電子顕微鏡によるソフトマテリアル可視化に向けた取り組み招待有り

濵口祐

クライオ電子顕微鏡・技術説明会　2024年2月14日
Investigation and application of solvent effects in high-resolution single-particle cryogenic-electron microscopy 国際会議

Keigo Oka, Tasuku Hamaguchi, Daisuke Unabara, Koji Yonekura

2023年12月11日
Cryo-EM observation of wide range of soft-materials 国際会議招待有り

Tasuku Hamaguchi, Keisuke Kawakami, Daisuke Unabara, Koji Yonekura

第61回生物物理学会年会台湾-日本二国間シンポジウム　2023年11月14日
多様な液体材料観察を可能とするクライオEM試料作製法の検討とトモグラフィー解析

海原大輔, 浜口祐, 米倉功治

日本顕微鏡学会第66回シンポジウム　2023年11月12日
アキラルCo(Ⅱ)フタロシアニンで構成された螺旋超分子のMC-AFMによる電流測定

相澤洋紀, 佐藤拓朗, 米倉功治, 米倉‐眞木沙織, 濱口祐, 高場圭章, 湊丈俊, 山本浩史

第17回分子科学討論会2023大阪　2023年9月13日
Cryo-EM observation of γ-polyglutamic acid hydrogels from Bacillus subtilis of Firmicutes 国際会議

Tasuku Hamaguchi, Daisuke Unabara, Koji Yonekura

24th Biennial Congress of the International Organization for Mycoplasmology (IOM)　2023年7月17日
Cryo-EM observations for proteins and soft-materials 招待有り

Tasuku Hamaguchi, Keisuke Kawakami, Daisuke Unabara, Koji Yonekura

日本顕微鏡学会第７９回学術講演会国際サテライトシンポジウム　2023年6月25日
多元物質科学研究所におけるクライオ電子顕微鏡を用いた取り組み（利用方法から観察事例まで）招待有り

浜口祐

2022年度東北大学多元物質科学研究所イノベーションエクスチェンジ　2023年1月18日
CRYO ARMオーナーズMTG 招待有り

浜口祐

第一回CRYO ARMオーナーズMTG　2022年12月26日
Core and rod structures of a thermophilic cyanobacterial light-harvesting phycobilisome

Keisuke Kawakami, Tasuku Hamaguchi, Yuu Hirose, Daisuke Kosumi, Makoto Miyata, Nobuo Kamiya, Koji Yonekura

AsBIC10 2022　2022年11月30日
Analysis of Japanese sake using synchrotron light and cryo-TEM 招待有り

Tasuku Hamaguchi

2022年11月25日
理研・東北大の施設報告

浜口祐

AMED/BINDS第1回クライオ電子顕微鏡施設技術交流会　2022年11月21日
高精度クライオEMによる構造解析招待有り

浜口祐

生理研研究会「新世代のクライオ電子顕微鏡」　2022年11月1日
電子線照射に極めて弱い補酵素のクライオEM単粒子構造解析招待有り

浜口祐

生理研研究会「新世代のクライオ電子顕微鏡」　2022年11月1日
CYPを対象としたCryo-EM 招待有り

米倉功治, 浜口祐, 高場圭章, 川上恵典, 眞木さおり

CBI学会2022年大会　2022年10月25日
クライオ電子顕微鏡による高精度構造解析

浜口祐, 川上恵介, 眞木さおり, 米倉功治

第60回日本生物物理学会年会　2022年9月30日
ソフトマテリアル研究拠点：創薬

浜口祐

ソフトマテリアル研究拠点会議　2022年8月10日
High-resolution and high-precision cryo-ED and EM 招待有り

Yonekura K, Maki-Yonekura S, Takaba K, Hamaguchi T, Naitow H, Kawakami K

Biological Structural Dynamics by Ultrafast X-ray and 4D Electron Microscopy, Pacifichem 2021　2021年12月16日
The development of 3D ED on studying structure and charge state of protein microcrystals 国際会議招待有り

Yonekura K, Maki-Yonekura S, Takaba K, Hamaguchi T, Naitow H, Kawakami K

25th IUCr Congress Satellite School on Electron Crystallography　2021年8月11日
Complementary use of high-resolution and high-precision cryo-ED and EM 招待有り

Yonekura K, Maki-Yonekura S, Takaba K, Hamaguchi T, Naitow H, Kawakami K

Microscopy and Microanalysis (M&M) 2021　2021年8月2日
Cryo-ED and EM for higher-resolution and higher-precision structure analysis 招待有り

Yonekura, K, Maki-Yonekura, S. Hamaguchi, T, Naitow, H, Kiyofumi, T

Japan-Canada Joint Symposium 2020, Development and applications of the methods combining interference/phase measurement techniques and analytic techniques, Japanese Society of Microscopy　2020年5月26日
Cryo-ED and EM for Higher-Resolution and Higher-Precision Structures 招待有り

Yonekura K, Maki-Yonekura S, Hamaguchi T, Naitow H, Takaba K

12th Asia-Pacific Microscopy Conference (APMC2020) Hyderabad International Convention Center, Hyderabad, India　2020年2月4日

︎全件表示 ︎最初の5件までを表示

産業財産権 1

立体模型の製造方法、及び立体模型

浜口祐, 宮田真人

産業財産権の種類: 特許権

共同研究・競争的資金等の研究課題 4

安全かつ効率的なCas3ゲノム編集ツール開発に資する機能構造相関研究

竹下浩平, 浜口祐, 清水伸隆, 吉見一人

2024年4月1日～ 2025年3月31日
安全かつ効率的なCas3ゲノム編集ツール開発に資する機能構造相関研究

竹下浩平, 浜口祐, 清水伸隆, 吉見一人

提供機関：Japan Society for the Promotion of Science

制度名：Grants-in-Aid for Scientific Research

研究種目：Grant-in-Aid for Scientific Research (B)

研究機関：Institute of Physical and Chemical Research

2022年4月1日～ 2025年3月31日
エクソソーム局在性膜タンパク質EAAC1およびCD63の構造解析

浜口祐

提供機関：Japan Society for the Promotion of Science

制度名：Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)

研究種目：Grant-in-Aid for Scientific Research (C)

研究機関：Institute of Physical and Chemical Research

2020年4月～ 2023年3月

詳細を見る詳細を閉じる

マウス由来グルタミン酸トランスポーター（EAAC1）について，Expi293F株を用いた高発現系の確立と，精製法の最適化を行った．EAAC1はグルタミン酸だけでなく，システインの輸送にも関わることが提唱されており，その輸送機構の解明を目指し，システイン存在下での精製を行った．また同時にクライオ電子顕微鏡撮影において妨げとなる塩，界面活性剤，安定化剤などの低濃度条件下において，EAAC1をmg/mlオーダーにて精製することに成功した．また，界面活性剤とともに共存する脂質量を調製することで，濃縮効率と安定性が改善された．得られたEAAC1を用いて，ネガティブ染色電子顕微鏡観察法により粒子の可視化を試みたところ，均一性が評価でき，得られた粒子のサイズ分布はEAAC1が３量体で存在する際に想定される粒子径とおおむね同じであった．このことから，EAAC1が本来の機能を維持した状態で精製できたものと考えられた．このように調製したEAAC1についてクライオ電子顕微鏡構造解析に向けて様々なグリッド作成条件を検討を行ったところグルタミン酸輸送体と思われる像の撮影に成功した．また，粒子には界面活性剤に由来すると考えられるミセルバンド像も見られた．しかし，界面活性剤存在下でのグリッド作成時に頻出する粒子の低分布・低密度化が生じており，さらなる高濃度化が必要であると考えられた．現在までにサンプルの培養，可溶化，精製を繰り返し，構造解析を実現可能な量の試料調製を行った．また，テトラスパニンについては細胞中での高発現が確認できており，様々な可溶化，製紙恵方を試みたが，現在までに均一なタンパク質粒子としては得られていない．
機能性人工核酸のロジカル設計・創出技術の実現と未来型医療の開拓

2021年4月～ 2022年3月