Result

宇宙実験の成果

02

宇宙実験の成果をご紹介します（今後、随時更新予定）。

成果報告・プレスリリース等

これまでの品質向上事例については以下もご参照ください。

多くのタンパク質で地上より高品質の結晶生成に成功、薬剤候補化合物との結合状態解明も多数

主要論文リスト

  • Sakamoto Y, Suzuki Y, Nakamura A, Watanabe Y, Sekiya M, Roppongi S, Kushibiki C, Iizuka I, Tani O, Sakashita H, Inaka K, Tanaka H, Yamada M, Ohta K, Honma N, Shida Y, Ogasawara W, Nakanishi-Matsui M, Nonaka T, Gouda H & Tanaka N. Fragment-based discovery of the first nonpeptidyl inhibitor of an S46 family peptidase. Scientific Reports volume 9, Article number: 13587 (2019)
    https://doi.org/10.1038/s41598-019-49984-3
  • Morita Y, Yamada T, Kureishi M, Kihira K, Komatsu T. Quaternary Structure Analysis of a Hemoglobin Core in Hemoglobin-Albumin Cluster. J Phys Chem B. 2018 Dec 20;122(50):12031-12039.
    https://doi.org/10.1021/acs.jpcb.8b10077
  • Hatae H, Inaka K, Okamura R, Furubayashi N, Kamo M, Kobayashi T, Abe Y, Iwata S, Hamasaki N. Crystallization of human erythrocyte Band 3, the anion exchanger, at the International Space Station "KIBO″. Analytical Biochemistry. 2018 October 15; 559: 91-93.
    https://doi.org/10.1016/j.ab.2018.08.009
  • Nakae S, Shionyu M, Ogawa T, Shirai T. Structures of jacalin-related lectin PPL3 regulating pearl shell biomineralization. Proteins. 2018 Jun;86(6):644-653.
    https://doi.org/10.1002/prot.25491
  • Yokomaku K, Akiyama M, Morita Y, Kihira K, Komatsu T. Core-shell protein cluster comprising haemoglobin and recombinant feline serum albumin as an artificial O2 carrier for cats. Journal of Materials Chemistry B. 2018 March 20; 6: 2417-2425.
    https://doi.org/10.1039/C8TB00211H
  • Negoro S, Shibata N, Lee Y, Takehara I, Kinugasa R, Nagai K. Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase. Scientific Reports volume 8, Article number: 9725 (2018)
    https://doi.org/10.1038/s41598-018-27860-w
  • Kinoshita T, Hashimoto T, Sogabe Y, Fukada H, Matsumoto T, Sawa M. High-resolution structure discloses the potential for allosteric regulation of mitogen-activated protein kinase kinase 7. Biochemical and Biophysical Research Communications. 2017 November 4; 493(1): 313-317.
    https://doi.org/10.1016/j.bbrc.2017.09.025
  • Itoh T, Hibi T, Suzuki F, Sugimoto I, Fujiwara A, Inaka K, Tanaka H, Ohta K, Fujii Y, Taketo A, Kimoto H. Crystal structure of chitinase ChiW from Paenibacillus sp. str. FPU-7 reveals a novel type of bacterial cell-surface-expressed multi-modular enzyme machinery. PLOS ONE. 2016 December 1; 11(12): e0167310.
    https://doi.org/10.1371/journal.pone.0167310
  • Yoshida H, Yoshihara A, Ishii T, Izumori K, Kamitori S. X-ray structures of the Pseudomonas cichorii D-tagatose 3-epimerase mutant form C66S recognizing deoxy sugars as substrates. Applied Microbiology and Biotechnology. 2016 July; epub: 13 pp.
    https://doi.org/10.1007/s00253-016-7673-7
  • Nakamura A, Ishida T, Kusaka K, Yamada T, Fushinobu S, Tanaka I, Kaneko S, Ohta K, Tanaka H, Inaka K, Higuchi Y, Niimura N, Samejima M, Igarashi K. "Newton's cradle" proton relay with amide-imidic acid tautomerization in inverting cellulase visualized by neutron crystallography. Science Advances. 2015 August 21; 1(7): e1500263-e1500263.
    https://doi.org/10.1126/sciadv.1500263
  • Sakamoto Y, Suzuki Y, Iizuka I, Tateoka C, Roppongi S, Fujimoto M, Inaka K, Tanaka H, Yamada M, Ohta K, Gouda H, Nonaka T, Ogasawara W, Tanaka N.Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity. Scientific Reports. 2015 Jun 9; 5:11151.
    https://doi.org/10.1038/srep11151
  • Sakamoto Y, Suzuki Y, Iizuka I, Tateoka C, Roppongi S, Fujimoto M, Inaka K, Tanaka H, Masaki M, Ohta K, Okada H, Nonaka T, Morikawa Y, Nakamura KT, Ogasawara W, Tanaka N. S46 peptidases are the first exopeptidases to be members of clan PA. Scientific Reports. 2014 May 15; 4: 4977.
    https://doi.org/10.1038/srep04977
  • Tanaka H, Sasaki S, Takahashi S, Inaka K, Wada Y, Yamada M, Ohta K, Miyoshi H, Kobayashi T, Kamigaichi S. Numerical model of protein crystal growth in a diffusive field such as the microgravity environment. Journal of Synchrotron Radiation. 2013 Nov; 20(Pt 6):1003-9.
    https://doi.org/10.1107/S0909049513022784
  • Takahashi S, Ohta K, Furubayashi N, Yan B, Koga M, Wada Y, Yamada M, Inaka K, Tanaka H, Miyoshi H, Kobayashi T, Kamigaichi S. JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals. Journal of Synchrotron Radiation. 2013 Nov; 20(Pt 6):968-73.
    https://doi.org/10.1107/S0909049513021596
  • Inaka K, Tanaka H, Takahashi S, Sano S, Sato M, Shirakawa M, Yoshimura Y. Numerical analysis of the diffusive field around a growing protein crystal in microgravity. Defect and Diffusion Forum. 2012 April; 323-325: 565-569.
    https://doi.org/10.4028/www.scientific.net/DDF.323-325.565
  • Tanaka H, Inaka K, Furubayashi N, Yamanaka M, Takahashi S, Sano S, Sato M, Shirakawa M, Yoshimura Y. Controlling the diffusive field to grow a higher quality protein crystal in microgravity. Defect and Diffusion Forum. 2012 April; 323-325: 549-554.
    https://doi.org/10.4028/www.scientific.net/DDF.323-325.549
  • Nakano H, Hosokawa A, Tagawa R, Inaka K, Ohta K, Nakatsu T, Kato H, Watanabe K. Crystallization and preliminary X-ray crystallographic analysis of Pz peptidase B from Geobacillus collagenovorans MO-1. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2012; 68: 757-759.
    https://doi.org/10.1107/S1744309112018969
  • Inaka K, Takahashi S, Aritake K, Tsurumura T, Furubayashi N, Yan B, Hirota E, Sano S, Sato M, Kobayashi T, Yoshimura Y, Tanaka H, Urade Y. High-Quality Protein Crystal Growth of Mouse Lipocalin-Type Prostaglandin D Synthase in Microgravity. Crystal Growth and Design. 2011 June; 11(6): 2107-2111.
    https://doi.org/10.1021/cg101370v
  • Tanaka H, Tsurumura T, Aritake K, Furubayashi N, Takahashi S, Yamanaka M, Hirota E, Sano S, Sato M, Kobayashi T, Tanaka T, Inaka K, Urade Y. Improvement in the quality of hematopoietic prostaglandin D synthase crystals in a microgravity environment. Journal of Synchrotron Radiation. 2011 January 1; 18(1): 88-91.
    https://doi.org/10.1107/S0909049510037076
  • Yamanaka M, Inaka K, Furubayashi N, Matsushima M, Takahashi S, Tanaka H, Sano S, Sato M, Kobayashi T, Tanaka T. Optimization of salt concentration in PEG-based crystallization solutions. Journal of Synchrotron Radiation. 2011 Jan; 18(1):84-7.
    https://doi.org/10.1107/S0909049510035995
  • Kamauchi S, Urade Y. Hematopoietic prostaglandin D synthase inhibitors for the treatment of duchenne muscular dystrophy. Brain and Nerve. 2011; 63(11): 1261-1269. PMID: 22068479. [Japanese]
  • Yamanaka M, Inaka K, Furubayashi N, Matsushima M, Takahashi S, Tanaka H, Sano S, Sato M, Kobayashi T, Tanaka T. Optimization of salt concentration in PEG-based crystallization solutions. Journal of Synchrotron Radiation. 2011; 18: 84-87.
    https://doi.org/10.1107/S0909049510035995
  • Oda K, Matoba Y, Noda M, Kumagai T, Sugiyama M. Catalytic Mechanism of Bleomycin N-Acetyl- transferase Proposed on the Basis of Its Crystal Structure, Journal of Biological Chemistry. 2010 Jan 8; 285(2):1446-56.
    https://doi.org/10.1074/jbc.M109.022277
  • Takahashi S, Tsurumura T, Aritake K, Furubayashi N, Sato M, Yamanaka M, Hirota E, Sano S, Kobayashi T, Tanaka T, Inaka K, Tanaka H, Urade Y. High-quality crystals of human haematopoietic prostaglandin D synthase with novel inhibitors. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2010; 66(Pt. 7): 846-850.
    https://doi.org/10.1107/S1744309110020828
  • Higashiura A, Kurakane T, Matsuda M, Suzuki M, Kobayashi T, Tanaka T, Tanaka H, Fujiwara T, Nakagawa A. High-resolution X-ray crystal structure of bovine H-protein at 0.88 A resolution. Acta Crystallographica Section D: Biological Crystallography. 2010; 66: 698-708.
    https://doi.org/10.1107/S0907444910010668
  • Tanaka H, Umehara T, Inaka K, Takahashi S, Shibata R, Bessho Y, Sato M, Sugiyama S, Fusatomi E, Terada T, Shirouzu M, Sano S, Motohara M, Kobayashi T, Tanaka T, Tanaka A, Yokoyama S. Crystallization of the archaeal transcription termination factor NusA: a significant decrease in twinning under microgravity conditions. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2007 01/17/2007; 63(2): 69-73.
    https://doi.org/10.1107/S1744309106054625
  • Sato M, Tanaka H, Inaka K, Shinozaki S, Yamanaka A, Takahashi S, Yamanaka M, Hirota E, Sugiyama S, Kato M, Saito C, Sano S, Motohara M, Nakamura T, Kobayashi T, Yoshitomi S, Tanaka T. JAXA-GCF project - high-quality protein crystals grown under microgravity environment for better understanding of protein structure. Microgravity Science and Technology. 2006 September; 18(3/4): 184-189.
    https://doi.org/10.1007/BF02870406
  • Kitatani T, Nakamura Y, Wada K, Kinoshita T, Tamoi M, Shigeoka S, Tada T. Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006; 62: 727-730.
    https://doi.org/10.1107/S1744309106027916
  • Tanaka H, Yoshizaki I, Takahashi S, Yamanaka M, Fukuyama S, Sato M, Sano S, Motohara M, Kobayashi T, Yoshitomi S, Tanaka T. Diffusion Coefficient of the Protein in Various Crystallization Solutions: The Key to Growing High-quality Crystals in Space. Microgravity Science and Technology. 2006; 18(3/4): 91-94.
    https://doi.org/10.1007/BF02870387
  • Kinoshita T, Maruki R, Warizaya M, Nakajima H, Nishimura S. Structure of a high-resolution crystal form of human trisephosphate isomerase: improvement of crystals using the gel tube method. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2005; 61: 346-349.
    https://doi.org/10.1107/S1744309105008341
  • Tanaka H, Inaka K, Sugiyama S, Takahashi S, Sano S, Sato M, Yoshitomi S. Numerical Analysis of the Depletion Zone Formation Around a Growing Protein Crystal. Annals of the New York Academy of Sciences. 2004; 1027: 10-19.
    https://doi.org/10.1196/annals.1324.002
  • Yoshizaki I, Nakamura H, Fukuyama S, Yoda S, Komatsu H, "Scientific approach on the optimization of protein crystallization condition for microgravity experiments" New York Academy of Sciences Vol. 1027 (2004) 28-47.
    https://doi.org/10.1196/annals.1324.004

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