Japan Aerospace Exploration Agency Protein Crystal Growth (JAXA PCG) - 04.09.15
The High Quality Protein Crystal Growth Experiment (JAXA PCG) aims at the growth of crystals of biological macromolecules by the counter-diffusion technique. The main scientific objective of the JAXA PCG experiment is to make high quality protein crystals under microgravity environment. Science Results for Everyone
Protein crystallization experiments have been performed in space for more than 20 years. In this experiment, more than 300 protein samples are launched and high quality crystals successfully grown from about 80 percent of them. It is expected that a protein depletion zone and an impurity depletion zone are formed around a crystal during protein crystal growth if the process is not disturbed by gravity, thus giving better quality crystals. A new technique to estimate growth rate and impurity proves that, in microgravity, protein depletion and impurity depletion zones appear. Detailed analysis of high quality protein crystal structures is useful in designing new pharmaceuticals and catalysts for a wide range of industries. Experiment Details
OpNom: JAXA PCG
Japan Aerospace Exploration Agency (JAXA), Tsukuba, Japan
Sponsoring Space Agency
Japan Aerospace Exploration Agency (JAXA)
ISS Expedition Duration
March 2009 - Ongoing
Previous ISS Missions
The precursor to JAXA PCG, JAXA GCF was completed in Russian Service Module from 2003 to 2008. ^ back to top
- Under microgravity conditions, convection and sedimentation are suppressed. Therefore, diffusion areas are maintained, the density around the crystals decreases, the crystals grow slowly, the capture of impurities and microcrystal decreases, and a crystal will grow well.
- High quality protein crsystals are obtained.
- Using high quality crystals obtained in the space experiment, detailed information on crystal structures for designing new drugs for diseases and catalysts for ecological application are obtained.
JAXA has developed a new technique that estimates the driving force ratio of crystals grown on the ground and in space, and the capture ratio of impurities through the diffusion/capture coefficient of protein. This technique proved that under microgravity conditions with high viscosity and slow diffusion, a protein depletion zone and impurity depletion zone appears. Using this technique researchers try to get high quality protein crystals. The goal is to contribute to yielding results which meet the social requirements.
The growth of protein crystals on board ISS shows the benefits of utilizing the ISS as a platform for microgravity science and research.
This experiment contributes to society by space-grown protein crystals being used to help create new drugs for diseases, as well as the development of new catalysts for use in the industrial and energy sectors.
Module within 24 hrs. The PCRF controls the temperature at 20°C. After the experiment is done, the crew removes the PCG Canisters from the PCRF cell tray, and packs Canisters for return and retrieval from Soyuz within 12 hours after landing.
Loading of the protein samples into the crystallization cells is done in Japan or Russia (Moscow). Installation of crystallization cells into the Crystallization Cannister at the Baikonur launch site is done, and launched on Soyuz/Progress. After docking to ISS, the crew transfers the canisters to Kibo. The crew installs canisters into the cell tray of the Protein Crystallization Research Facility (PCRF), and starts and runs the experiment for 42 to 120 days at 20°C. Crystal Growth starts automatically from the ground, no crew interaction is required. At the completion of the experiment, the crew removes canisters from the PCRF cell tray and packs the canisters for return and retrieval on Soyuz. The 3D structure of the protein crystals grown in space are analyzed at a synchrotron facility on the ground.ground.
Protein crystallization experiment in space environment has been performed for more than 20 years. JAXA has conducted protein crystallization experiment in ISS since 2003. In this experiment, totally over 300 protein samples were launched by Russian space transportation system and JAXA developed the technology to obtain the high quality crystals in space. JAXA also established user-friendly support service system for users to apply to the space experiment easily.About 80% proteins were crystallized in past JAXA PCG mission. This ratio is almost equal to the past protein crystallization experiment of JAXA.The excellent diffraction data to be able to analyze the protein structure newly was obtained for three kinds of proteins. Now detaled structure analysis of those proteins are conducted. The space-grown crystals will be applied structural biology and pharmaceutical activity.^ back to top
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. DOI: 10.1107/S1744309110020828.
Safonova TN, Mordkovich NN, Polyakov KM, Manuvera VA, Veiko VP, Popov VO. Crystallization of uridine phosphorylase from Shewanella oneidensis MR-1 in the laboratory and under microgravity and preliminary X-ray diffraction analysis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2012 10/30/2012; 68(11): 1387-1389. DOI: 10.1107/S1744309112041784. PMID: 23143255.
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. DOI: Defect and Diffusion Forum.
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. DOI: 10.4028/www.scientific.net/DDF.323-325.565.
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. DOI: 10.1107/S0909049510037076.
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. DOI: 10.1107/S1744309112018969.
Rahman RN, Ali MS, Leow TC, Salleh AB, Basri M, Matsumura H. The Effects of Microgravity on Thermostable T1 Lipase Protein Crystal. Gravitational and Space Biology. 2010; 23(2): 89-90.
Aris SN, Chor AL, Ali MS, Basri M, Salleh AB, Rahman RN. Crystallographic analysis of ground and space thermostable T1 lipase crystal obtained via counter diffusion method approach. BioMed Research International. 2014; 2014(904381): 8 pp. DOI: 10.1155/2014/904381.
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. DOI: 10.1021/cg101370v.
Ground Based Results Publications
Timofeev V, Smirnova E, Chupova L, Esipov R, Kuranova IP. X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction. Acta Crystallographica Section D: Biological Crystallography. 2012 11/09/2012; 68(12): 1660-1670. DOI: 10.1107/S0907444912040206.
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 October 1; 20(6). DOI: 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 November; 20(6): 968-973. DOI: 10.1107/S0909049513021596.
High Quality Protein Crystallization Research (HQPC)
Protein Crystallization Research Facility. Image courtesy of JAXA.
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High Quality Protein Crystal Growth Experiment Canister. Image courtesy of JAXA.
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NASA Image: ISS022E057676 - View of Japan Aerospace Exploration Agency (JAXA) Soichi Noguchi, Expedition 22 Flight Engineer (FE), during installation of Protein Crystal Growth (PCG) canister into the Protein Crystallization Research Facility (PCRF).
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