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Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality
High-quality protein crystals of suitable size are an important prerequisite for applying X-ray crystallography to determine the 3-dimensional structure of proteins. However, it is often difficult to obtain protein crystals of appropriate size and quality because nucleation and growth processes can...
Autores principales: | , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4255177/ https://www.ncbi.nlm.nih.gov/pubmed/25471817 http://dx.doi.org/10.1038/srep07308 |
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author | Guo, Yun-Zhu Sun, Li-Hua Oberthuer, Dominik Zhang, Chen-Yan Shi, Jian-Yu Di, Jiang-Lei Zhang, Bao-Liang Cao, Hui-Ling Liu, Yong-Ming Li, Jian Wang, Qian Huang, Huan-Huan Liu, Jun Schulz, Jan-Mirco Zhang, Qiu-Yu Zhao, Jian-Lin Betzel, Christian He, Jian-Hua Yin, Da-Chuan |
author_facet | Guo, Yun-Zhu Sun, Li-Hua Oberthuer, Dominik Zhang, Chen-Yan Shi, Jian-Yu Di, Jiang-Lei Zhang, Bao-Liang Cao, Hui-Ling Liu, Yong-Ming Li, Jian Wang, Qian Huang, Huan-Huan Liu, Jun Schulz, Jan-Mirco Zhang, Qiu-Yu Zhao, Jian-Lin Betzel, Christian He, Jian-Hua Yin, Da-Chuan |
author_sort | Guo, Yun-Zhu |
collection | PubMed |
description | High-quality protein crystals of suitable size are an important prerequisite for applying X-ray crystallography to determine the 3-dimensional structure of proteins. However, it is often difficult to obtain protein crystals of appropriate size and quality because nucleation and growth processes can be unsuccessful. Here, we show that by adsorbing proteins onto porous polystyrene-divinylbenzene microspheres (SDB) floating on the surface of the crystallisation solution, a localised high supersaturation region at the surface of the microspheres and a low supersaturation region below the microspheres can coexist in a single solution. The crystals will easily nucleate in the region of high supersaturation, but when they grow to a certain size, they will sediment to the region of low supersaturation and continue to grow. In this way, the probability of crystallisation and crystal quality can be simultaneously increased in a single solution without changing other crystallisation parameters. |
format | Online Article Text |
id | pubmed-4255177 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-42551772014-12-08 Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality Guo, Yun-Zhu Sun, Li-Hua Oberthuer, Dominik Zhang, Chen-Yan Shi, Jian-Yu Di, Jiang-Lei Zhang, Bao-Liang Cao, Hui-Ling Liu, Yong-Ming Li, Jian Wang, Qian Huang, Huan-Huan Liu, Jun Schulz, Jan-Mirco Zhang, Qiu-Yu Zhao, Jian-Lin Betzel, Christian He, Jian-Hua Yin, Da-Chuan Sci Rep Article High-quality protein crystals of suitable size are an important prerequisite for applying X-ray crystallography to determine the 3-dimensional structure of proteins. However, it is often difficult to obtain protein crystals of appropriate size and quality because nucleation and growth processes can be unsuccessful. Here, we show that by adsorbing proteins onto porous polystyrene-divinylbenzene microspheres (SDB) floating on the surface of the crystallisation solution, a localised high supersaturation region at the surface of the microspheres and a low supersaturation region below the microspheres can coexist in a single solution. The crystals will easily nucleate in the region of high supersaturation, but when they grow to a certain size, they will sediment to the region of low supersaturation and continue to grow. In this way, the probability of crystallisation and crystal quality can be simultaneously increased in a single solution without changing other crystallisation parameters. Nature Publishing Group 2014-12-04 /pmc/articles/PMC4255177/ /pubmed/25471817 http://dx.doi.org/10.1038/srep07308 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 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 in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/4.0/ |
spellingShingle | Article Guo, Yun-Zhu Sun, Li-Hua Oberthuer, Dominik Zhang, Chen-Yan Shi, Jian-Yu Di, Jiang-Lei Zhang, Bao-Liang Cao, Hui-Ling Liu, Yong-Ming Li, Jian Wang, Qian Huang, Huan-Huan Liu, Jun Schulz, Jan-Mirco Zhang, Qiu-Yu Zhao, Jian-Lin Betzel, Christian He, Jian-Hua Yin, Da-Chuan Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality |
title | Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality |
title_full | Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality |
title_fullStr | Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality |
title_full_unstemmed | Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality |
title_short | Utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality |
title_sort | utilisation of adsorption and desorption for simultaneously improving protein crystallisation success rate and crystal quality |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4255177/ https://www.ncbi.nlm.nih.gov/pubmed/25471817 http://dx.doi.org/10.1038/srep07308 |
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