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The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography
Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on...
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/PMC5069500/ https://www.ncbi.nlm.nih.gov/pubmed/27756898 http://dx.doi.org/10.1038/srep35279 |
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author | Edlund, Petra Takala, Heikki Claesson, Elin Henry, Léocadie Dods, Robert Lehtivuori, Heli Panman, Matthijs Pande, Kanupriya White, Thomas Nakane, Takanori Berntsson, Oskar Gustavsson, Emil Båth, Petra Modi, Vaibhav Roy-Chowdhury, Shatabdi Zook, James Berntsen, Peter Pandey, Suraj Poudyal, Ishwor Tenboer, Jason Kupitz, Christopher Barty, Anton Fromme, Petra Koralek, Jake D. Tanaka, Tomoyuki Spence, John Liang, Mengning Hunter, Mark S. Boutet, Sebastien Nango, Eriko Moffat, Keith Groenhof, Gerrit Ihalainen, Janne Stojković, Emina A. Schmidt, Marius Westenhoff, Sebastian |
author_facet | Edlund, Petra Takala, Heikki Claesson, Elin Henry, Léocadie Dods, Robert Lehtivuori, Heli Panman, Matthijs Pande, Kanupriya White, Thomas Nakane, Takanori Berntsson, Oskar Gustavsson, Emil Båth, Petra Modi, Vaibhav Roy-Chowdhury, Shatabdi Zook, James Berntsen, Peter Pandey, Suraj Poudyal, Ishwor Tenboer, Jason Kupitz, Christopher Barty, Anton Fromme, Petra Koralek, Jake D. Tanaka, Tomoyuki Spence, John Liang, Mengning Hunter, Mark S. Boutet, Sebastien Nango, Eriko Moffat, Keith Groenhof, Gerrit Ihalainen, Janne Stojković, Emina A. Schmidt, Marius Westenhoff, Sebastian |
author_sort | Edlund, Petra |
collection | PubMed |
description | Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the room temperature crystal structure of the chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 Å resolution. The structure was obtained by serial femtosecond X-ray crystallography from microcrystals at an X-ray free electron laser. We find overall good agreement compared to a crystal structure at 1.35 Å resolution derived from conventional crystallography at cryogenic temperatures, which we also report here. The thioether linkage between chromophore and protein is subject to positional ambiguity at the synchrotron, but is fully resolved with SFX. The study paves the way for time-resolved structural investigations of the phytochrome photocycle with time-resolved SFX. |
format | Online Article Text |
id | pubmed-5069500 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-50695002016-10-26 The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography Edlund, Petra Takala, Heikki Claesson, Elin Henry, Léocadie Dods, Robert Lehtivuori, Heli Panman, Matthijs Pande, Kanupriya White, Thomas Nakane, Takanori Berntsson, Oskar Gustavsson, Emil Båth, Petra Modi, Vaibhav Roy-Chowdhury, Shatabdi Zook, James Berntsen, Peter Pandey, Suraj Poudyal, Ishwor Tenboer, Jason Kupitz, Christopher Barty, Anton Fromme, Petra Koralek, Jake D. Tanaka, Tomoyuki Spence, John Liang, Mengning Hunter, Mark S. Boutet, Sebastien Nango, Eriko Moffat, Keith Groenhof, Gerrit Ihalainen, Janne Stojković, Emina A. Schmidt, Marius Westenhoff, Sebastian Sci Rep Article Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the room temperature crystal structure of the chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 Å resolution. The structure was obtained by serial femtosecond X-ray crystallography from microcrystals at an X-ray free electron laser. We find overall good agreement compared to a crystal structure at 1.35 Å resolution derived from conventional crystallography at cryogenic temperatures, which we also report here. The thioether linkage between chromophore and protein is subject to positional ambiguity at the synchrotron, but is fully resolved with SFX. The study paves the way for time-resolved structural investigations of the phytochrome photocycle with time-resolved SFX. Nature Publishing Group 2016-10-19 /pmc/articles/PMC5069500/ /pubmed/27756898 http://dx.doi.org/10.1038/srep35279 Text en Copyright © 2016, The Author(s) 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 Edlund, Petra Takala, Heikki Claesson, Elin Henry, Léocadie Dods, Robert Lehtivuori, Heli Panman, Matthijs Pande, Kanupriya White, Thomas Nakane, Takanori Berntsson, Oskar Gustavsson, Emil Båth, Petra Modi, Vaibhav Roy-Chowdhury, Shatabdi Zook, James Berntsen, Peter Pandey, Suraj Poudyal, Ishwor Tenboer, Jason Kupitz, Christopher Barty, Anton Fromme, Petra Koralek, Jake D. Tanaka, Tomoyuki Spence, John Liang, Mengning Hunter, Mark S. Boutet, Sebastien Nango, Eriko Moffat, Keith Groenhof, Gerrit Ihalainen, Janne Stojković, Emina A. Schmidt, Marius Westenhoff, Sebastian The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography |
title | The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography |
title_full | The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography |
title_fullStr | The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography |
title_full_unstemmed | The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography |
title_short | The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography |
title_sort | room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5069500/ https://www.ncbi.nlm.nih.gov/pubmed/27756898 http://dx.doi.org/10.1038/srep35279 |
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