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Protein crystal screening and characterization for serial femtosecond nanocrystallography

The recent development of X-ray free electron lasers (XFELs) has spurred the development of serial femtosecond nanocrystallography (SFX) which, for the first time, is enabling structure retrieval from sub-micron protein crystals. Although there are already a growing number of structures published us...

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Autores principales: Darmanin, Connie, Strachan, Jamie, Adda, Christopher G., Ve, Thomas, Kobe, Bostjan, Abbey, Brian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4853777/
https://www.ncbi.nlm.nih.gov/pubmed/27139248
http://dx.doi.org/10.1038/srep25345
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author Darmanin, Connie
Strachan, Jamie
Adda, Christopher G.
Ve, Thomas
Kobe, Bostjan
Abbey, Brian
author_facet Darmanin, Connie
Strachan, Jamie
Adda, Christopher G.
Ve, Thomas
Kobe, Bostjan
Abbey, Brian
author_sort Darmanin, Connie
collection PubMed
description The recent development of X-ray free electron lasers (XFELs) has spurred the development of serial femtosecond nanocrystallography (SFX) which, for the first time, is enabling structure retrieval from sub-micron protein crystals. Although there are already a growing number of structures published using SFX, the technology is still very new and presents a number of unique challenges as well as opportunities for structural biologists. One of the biggest barriers to the success of SFX experiments is the preparation and selection of suitable protein crystal samples. Here we outline a protocol for preparing and screening for suitable XFEL targets.
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spelling pubmed-48537772016-05-16 Protein crystal screening and characterization for serial femtosecond nanocrystallography Darmanin, Connie Strachan, Jamie Adda, Christopher G. Ve, Thomas Kobe, Bostjan Abbey, Brian Sci Rep Article The recent development of X-ray free electron lasers (XFELs) has spurred the development of serial femtosecond nanocrystallography (SFX) which, for the first time, is enabling structure retrieval from sub-micron protein crystals. Although there are already a growing number of structures published using SFX, the technology is still very new and presents a number of unique challenges as well as opportunities for structural biologists. One of the biggest barriers to the success of SFX experiments is the preparation and selection of suitable protein crystal samples. Here we outline a protocol for preparing and screening for suitable XFEL targets. Nature Publishing Group 2016-05-03 /pmc/articles/PMC4853777/ /pubmed/27139248 http://dx.doi.org/10.1038/srep25345 Text en Copyright © 2016, Macmillan Publishers Limited 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
Darmanin, Connie
Strachan, Jamie
Adda, Christopher G.
Ve, Thomas
Kobe, Bostjan
Abbey, Brian
Protein crystal screening and characterization for serial femtosecond nanocrystallography
title Protein crystal screening and characterization for serial femtosecond nanocrystallography
title_full Protein crystal screening and characterization for serial femtosecond nanocrystallography
title_fullStr Protein crystal screening and characterization for serial femtosecond nanocrystallography
title_full_unstemmed Protein crystal screening and characterization for serial femtosecond nanocrystallography
title_short Protein crystal screening and characterization for serial femtosecond nanocrystallography
title_sort protein crystal screening and characterization for serial femtosecond nanocrystallography
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4853777/
https://www.ncbi.nlm.nih.gov/pubmed/27139248
http://dx.doi.org/10.1038/srep25345
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