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The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order
Cryocooling of macromolecular crystals is commonly employed to limit radiation damage during X-ray diffraction data collection. However, cooling itself affects macromolecular conformation and often damages crystals via poorly understood processes. Here, the effects of cryosolution thermal contractio...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6130464/ https://www.ncbi.nlm.nih.gov/pubmed/30198901 http://dx.doi.org/10.1107/S2059798318008793 |
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author | Juers, Douglas H. Farley, Christopher A. Saxby, Christopher P. Cotter, Rosemary A. Cahn, Jackson K. B. Holton-Burke, R. Conor Harrison, Kaitlin Wu, Zhenguo |
author_facet | Juers, Douglas H. Farley, Christopher A. Saxby, Christopher P. Cotter, Rosemary A. Cahn, Jackson K. B. Holton-Burke, R. Conor Harrison, Kaitlin Wu, Zhenguo |
author_sort | Juers, Douglas H. |
collection | PubMed |
description | Cryocooling of macromolecular crystals is commonly employed to limit radiation damage during X-ray diffraction data collection. However, cooling itself affects macromolecular conformation and often damages crystals via poorly understood processes. Here, the effects of cryosolution thermal contraction on macromolecular conformation and crystal order in crystals ranging from 32 to 67% solvent content are systematically investigated. It is found that the solution thermal contraction affects macromolecule configurations and volumes, unit-cell volumes, crystal packing and crystal order. The effects occur through not only thermal contraction, but also pressure caused by the mismatched contraction of cryosolvent and pores. Higher solvent-content crystals are more affected. In some cases the solvent contraction can be adjusted to reduce mosaicity and increase the strength of diffraction. Ice formation in some crystals is found to cause damage via a reduction in unit-cell volume, which is interpreted through solvent transport out of unit cells during cooling. The results point to more deductive approaches to cryoprotection optimization by adjusting the cryosolution composition to reduce thermal contraction-induced stresses in the crystal with cooling. |
format | Online Article Text |
id | pubmed-6130464 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-61304642018-09-17 The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order Juers, Douglas H. Farley, Christopher A. Saxby, Christopher P. Cotter, Rosemary A. Cahn, Jackson K. B. Holton-Burke, R. Conor Harrison, Kaitlin Wu, Zhenguo Acta Crystallogr D Struct Biol Research Papers Cryocooling of macromolecular crystals is commonly employed to limit radiation damage during X-ray diffraction data collection. However, cooling itself affects macromolecular conformation and often damages crystals via poorly understood processes. Here, the effects of cryosolution thermal contraction on macromolecular conformation and crystal order in crystals ranging from 32 to 67% solvent content are systematically investigated. It is found that the solution thermal contraction affects macromolecule configurations and volumes, unit-cell volumes, crystal packing and crystal order. The effects occur through not only thermal contraction, but also pressure caused by the mismatched contraction of cryosolvent and pores. Higher solvent-content crystals are more affected. In some cases the solvent contraction can be adjusted to reduce mosaicity and increase the strength of diffraction. Ice formation in some crystals is found to cause damage via a reduction in unit-cell volume, which is interpreted through solvent transport out of unit cells during cooling. The results point to more deductive approaches to cryoprotection optimization by adjusting the cryosolution composition to reduce thermal contraction-induced stresses in the crystal with cooling. International Union of Crystallography 2018-09-05 /pmc/articles/PMC6130464/ /pubmed/30198901 http://dx.doi.org/10.1107/S2059798318008793 Text en © Juers et al. 2018 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/ |
spellingShingle | Research Papers Juers, Douglas H. Farley, Christopher A. Saxby, Christopher P. Cotter, Rosemary A. Cahn, Jackson K. B. Holton-Burke, R. Conor Harrison, Kaitlin Wu, Zhenguo The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order |
title | The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order |
title_full | The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order |
title_fullStr | The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order |
title_full_unstemmed | The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order |
title_short | The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order |
title_sort | impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6130464/ https://www.ncbi.nlm.nih.gov/pubmed/30198901 http://dx.doi.org/10.1107/S2059798318008793 |
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