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In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth
Precise protein structure determination provides significant information on life science research, although high-quality crystals are not easily obtained. We developed a system for producing high-quality protein crystals with high throughput. Using this system, gravity-controlled crystallization are...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4768258/ https://www.ncbi.nlm.nih.gov/pubmed/26916802 http://dx.doi.org/10.1038/srep22127 |
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author | Nakamura, Akira Ohtsuka, Jun Kashiwagi, Tatsuki Numoto, Nobutaka Hirota, Noriyuki Ode, Takahiro Okada, Hidehiko Nagata, Koji Kiyohara, Motosuke Suzuki, Ei-ichiro Kita, Akiko Wada, Hitoshi Tanokura, Masaru |
author_facet | Nakamura, Akira Ohtsuka, Jun Kashiwagi, Tatsuki Numoto, Nobutaka Hirota, Noriyuki Ode, Takahiro Okada, Hidehiko Nagata, Koji Kiyohara, Motosuke Suzuki, Ei-ichiro Kita, Akiko Wada, Hitoshi Tanokura, Masaru |
author_sort | Nakamura, Akira |
collection | PubMed |
description | Precise protein structure determination provides significant information on life science research, although high-quality crystals are not easily obtained. We developed a system for producing high-quality protein crystals with high throughput. Using this system, gravity-controlled crystallization are made possible by a magnetic microgravity environment. In addition, in-situ and real-time observation and time-lapse imaging of crystal growth are feasible for over 200 solution samples independently. In this paper, we also report results of crystallization experiments for two protein samples. Crystals grown in the system exhibited magnetic orientation and showed higher and more homogeneous quality compared with the control crystals. The structural analysis reveals that making use of the magnetic microgravity during the crystallization process helps us to build a well-refined protein structure model, which has no significant structural differences with a control structure. Therefore, the system contributes to improvement in efficiency of structural analysis for “difficult” proteins, such as membrane proteins and supermolecular complexes. |
format | Online Article Text |
id | pubmed-4768258 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-47682582016-03-02 In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth Nakamura, Akira Ohtsuka, Jun Kashiwagi, Tatsuki Numoto, Nobutaka Hirota, Noriyuki Ode, Takahiro Okada, Hidehiko Nagata, Koji Kiyohara, Motosuke Suzuki, Ei-ichiro Kita, Akiko Wada, Hitoshi Tanokura, Masaru Sci Rep Article Precise protein structure determination provides significant information on life science research, although high-quality crystals are not easily obtained. We developed a system for producing high-quality protein crystals with high throughput. Using this system, gravity-controlled crystallization are made possible by a magnetic microgravity environment. In addition, in-situ and real-time observation and time-lapse imaging of crystal growth are feasible for over 200 solution samples independently. In this paper, we also report results of crystallization experiments for two protein samples. Crystals grown in the system exhibited magnetic orientation and showed higher and more homogeneous quality compared with the control crystals. The structural analysis reveals that making use of the magnetic microgravity during the crystallization process helps us to build a well-refined protein structure model, which has no significant structural differences with a control structure. Therefore, the system contributes to improvement in efficiency of structural analysis for “difficult” proteins, such as membrane proteins and supermolecular complexes. Nature Publishing Group 2016-02-26 /pmc/articles/PMC4768258/ /pubmed/26916802 http://dx.doi.org/10.1038/srep22127 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Nakamura, Akira Ohtsuka, Jun Kashiwagi, Tatsuki Numoto, Nobutaka Hirota, Noriyuki Ode, Takahiro Okada, Hidehiko Nagata, Koji Kiyohara, Motosuke Suzuki, Ei-ichiro Kita, Akiko Wada, Hitoshi Tanokura, Masaru In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth |
title | In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth |
title_full | In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth |
title_fullStr | In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth |
title_full_unstemmed | In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth |
title_short | In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth |
title_sort | in-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4768258/ https://www.ncbi.nlm.nih.gov/pubmed/26916802 http://dx.doi.org/10.1038/srep22127 |
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