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JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals
The Japan Aerospace Exploration Agency (JAXA) started a high-quality protein crystal growth project, now called JAXA PCG, on the International Space Station (ISS) in 2002. Using the counter-diffusion technique, 14 sessions of experiments have been performed as of 2012 with 580 proteins crystallized...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3795566/ https://www.ncbi.nlm.nih.gov/pubmed/24121350 http://dx.doi.org/10.1107/S0909049513021596 |
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author | Takahashi, Sachiko Ohta, Kazunori Furubayashi, Naoki Yan, Bin Koga, Misako Wada, Yoshio Yamada, Mitsugu Inaka, Koji Tanaka, Hiroaki Miyoshi, Hiroshi Kobayashi, Tomoyuki Kamigaichi, Shigeki |
author_facet | Takahashi, Sachiko Ohta, Kazunori Furubayashi, Naoki Yan, Bin Koga, Misako Wada, Yoshio Yamada, Mitsugu Inaka, Koji Tanaka, Hiroaki Miyoshi, Hiroshi Kobayashi, Tomoyuki Kamigaichi, Shigeki |
author_sort | Takahashi, Sachiko |
collection | PubMed |
description | The Japan Aerospace Exploration Agency (JAXA) started a high-quality protein crystal growth project, now called JAXA PCG, on the International Space Station (ISS) in 2002. Using the counter-diffusion technique, 14 sessions of experiments have been performed as of 2012 with 580 proteins crystallized in total. Over the course of these experiments, a user-friendly interface framework for high accessibility has been constructed and crystallization techniques improved; devices to maximize the use of the microgravity environment have been designed, resulting in some high-resolution crystal growth. If crystallization conditions were carefully fixed in ground-based experiments, high-quality protein crystals grew in microgravity in many experiments on the ISS, especially when a highly homogeneous protein sample and a viscous crystallization solution were employed. In this article, the current status of JAXA PCG is discussed, and a rational approach to high-quality protein crystal growth in microgravity based on numerical analyses is explained. |
format | Online Article Text |
id | pubmed-3795566 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-37955662013-10-15 JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals Takahashi, Sachiko Ohta, Kazunori Furubayashi, Naoki Yan, Bin Koga, Misako Wada, Yoshio Yamada, Mitsugu Inaka, Koji Tanaka, Hiroaki Miyoshi, Hiroshi Kobayashi, Tomoyuki Kamigaichi, Shigeki J Synchrotron Radiat Diffraction Structural Biology The Japan Aerospace Exploration Agency (JAXA) started a high-quality protein crystal growth project, now called JAXA PCG, on the International Space Station (ISS) in 2002. Using the counter-diffusion technique, 14 sessions of experiments have been performed as of 2012 with 580 proteins crystallized in total. Over the course of these experiments, a user-friendly interface framework for high accessibility has been constructed and crystallization techniques improved; devices to maximize the use of the microgravity environment have been designed, resulting in some high-resolution crystal growth. If crystallization conditions were carefully fixed in ground-based experiments, high-quality protein crystals grew in microgravity in many experiments on the ISS, especially when a highly homogeneous protein sample and a viscous crystallization solution were employed. In this article, the current status of JAXA PCG is discussed, and a rational approach to high-quality protein crystal growth in microgravity based on numerical analyses is explained. International Union of Crystallography 2013-11-01 2013-09-26 /pmc/articles/PMC3795566/ /pubmed/24121350 http://dx.doi.org/10.1107/S0909049513021596 Text en © Sachiko Takahashi et al. 2013 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Diffraction Structural Biology Takahashi, Sachiko Ohta, Kazunori Furubayashi, Naoki Yan, Bin Koga, Misako Wada, Yoshio Yamada, Mitsugu Inaka, Koji Tanaka, Hiroaki Miyoshi, Hiroshi Kobayashi, Tomoyuki Kamigaichi, Shigeki JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals |
title | JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals |
title_full | JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals |
title_fullStr | JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals |
title_full_unstemmed | JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals |
title_short | JAXA protein crystallization in space: ongoing improvements for growing high-quality crystals |
title_sort | jaxa protein crystallization in space: ongoing improvements for growing high-quality crystals |
topic | Diffraction Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3795566/ https://www.ncbi.nlm.nih.gov/pubmed/24121350 http://dx.doi.org/10.1107/S0909049513021596 |
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