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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...

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Autores principales: Juers, Douglas H., Farley, Christopher A., Saxby, Christopher P., Cotter, Rosemary A., Cahn, Jackson K. B., Holton-Burke, R. Conor, Harrison, Kaitlin, Wu, Zhenguo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2018
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.
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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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