A step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum

Using the UHV experimental endstation on the soft X-ray beamline at the Australian Synchrotron, lysozyme and proteinase K crystals have been exposed to a vacuum of 10(−5) mbar, prior to flash-cooling in a bath of liquid nitrogen. Subsequent data collection on the MX2 beamline at the Australian Synch...

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Detalles Bibliográficos
Autores principales: Panjikar, Santosh, Thomsen, Lars, O’Donnell, Kane Michael, Riboldi-Tunnicliffe, Alan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2015
Materias:
Short Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4453978/
https://www.ncbi.nlm.nih.gov/pubmed/26089765
http://dx.doi.org/10.1107/S1600576715006147
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author Panjikar, Santosh
Thomsen, Lars
O’Donnell, Kane Michael
Riboldi-Tunnicliffe, Alan
author_facet Panjikar, Santosh
Thomsen, Lars
O’Donnell, Kane Michael
Riboldi-Tunnicliffe, Alan
author_sort Panjikar, Santosh
collection PubMed
description Using the UHV experimental endstation on the soft X-ray beamline at the Australian Synchrotron, lysozyme and proteinase K crystals have been exposed to a vacuum of 10(−5) mbar, prior to flash-cooling in a bath of liquid nitrogen. Subsequent data collection on the MX2 beamline at the Australian Synchrotron demonstrated that, for lysozyme and proteinase K, it is possible to subject these mounted crystals to a vacuum pressure of 10(−5) mbar without destroying the crystal lattice. Despite the lower data quality of the vacuum-pumped crystals compared with control crystals, it is demonstrated that the protein crystals can survive in a vacuum under suitable conditions.
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spelling pubmed-44539782015-06-18 A step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum Panjikar, Santosh Thomsen, Lars O’Donnell, Kane Michael Riboldi-Tunnicliffe, Alan J Appl Crystallogr Short Communications Using the UHV experimental endstation on the soft X-ray beamline at the Australian Synchrotron, lysozyme and proteinase K crystals have been exposed to a vacuum of 10(−5) mbar, prior to flash-cooling in a bath of liquid nitrogen. Subsequent data collection on the MX2 beamline at the Australian Synchrotron demonstrated that, for lysozyme and proteinase K, it is possible to subject these mounted crystals to a vacuum pressure of 10(−5) mbar without destroying the crystal lattice. Despite the lower data quality of the vacuum-pumped crystals compared with control crystals, it is demonstrated that the protein crystals can survive in a vacuum under suitable conditions. International Union of Crystallography 2015-05-09 /pmc/articles/PMC4453978/ /pubmed/26089765 http://dx.doi.org/10.1107/S1600576715006147 Text en © Santosh Panjikar et al. 2015 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 Short Communications
Panjikar, Santosh
Thomsen, Lars
O’Donnell, Kane Michael
Riboldi-Tunnicliffe, Alan
A step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum
title A step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum
title_full A step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum
title_fullStr A step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum
title_full_unstemmed A step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum
title_short A step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum
title_sort step towards long-wavelength protein crystallography: subjecting protein crystals to a vacuum
topic Short Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4453978/
https://www.ncbi.nlm.nih.gov/pubmed/26089765
http://dx.doi.org/10.1107/S1600576715006147
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