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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...

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Autores principales: Takahashi, Sachiko, Ohta, Kazunori, Furubayashi, Naoki, Yan, Bin, Koga, Misako, Wada, Yoshio, Yamada, Mitsugu, Inaka, Koji, Tanaka, Hiroaki, Miyoshi, Hiroshi, Kobayashi, Tomoyuki, Kamigaichi, Shigeki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2013
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.
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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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