A bright and photostable photoconvertible fluorescent protein for fusion tags

Photoconvertible fluorescent proteins offer significant potential as tools for investigating dynamic processes in living cells and for emerging super-resolution microscopy techniques. Unfortunately, most probes in this class are hampered by oligomerization, small photon budgets, or poor photostabili...

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Detalles Bibliográficos
Autores principales: McKinney, Sean A., Murphy, Christopher S., Hazelwood, Kristin L., Davidson, Michael W., Looger, Loren L.
Formato: Texto
Lenguaje:English
Publicado: 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2745648/
https://www.ncbi.nlm.nih.gov/pubmed/19169260
http://dx.doi.org/10.1038/nmeth.1296
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author McKinney, Sean A.
Murphy, Christopher S.
Hazelwood, Kristin L.
Davidson, Michael W.
Looger, Loren L.
author_facet McKinney, Sean A.
Murphy, Christopher S.
Hazelwood, Kristin L.
Davidson, Michael W.
Looger, Loren L.
author_sort McKinney, Sean A.
collection PubMed
description Photoconvertible fluorescent proteins offer significant potential as tools for investigating dynamic processes in living cells and for emerging super-resolution microscopy techniques. Unfortunately, most probes in this class are hampered by oligomerization, small photon budgets, or poor photostability. Here we report an EosFP variant that functions well in a broad range of protein fusions for dynamic investigations, exhibits high photostability, and preserves the superior ~10-nm localization precision of its parent.
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spelling pubmed-27456482009-09-17 A bright and photostable photoconvertible fluorescent protein for fusion tags McKinney, Sean A. Murphy, Christopher S. Hazelwood, Kristin L. Davidson, Michael W. Looger, Loren L. Nat Methods Article Photoconvertible fluorescent proteins offer significant potential as tools for investigating dynamic processes in living cells and for emerging super-resolution microscopy techniques. Unfortunately, most probes in this class are hampered by oligomerization, small photon budgets, or poor photostability. Here we report an EosFP variant that functions well in a broad range of protein fusions for dynamic investigations, exhibits high photostability, and preserves the superior ~10-nm localization precision of its parent. 2009-01-25 2009-02 /pmc/articles/PMC2745648/ /pubmed/19169260 http://dx.doi.org/10.1038/nmeth.1296 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
McKinney, Sean A.
Murphy, Christopher S.
Hazelwood, Kristin L.
Davidson, Michael W.
Looger, Loren L.
A bright and photostable photoconvertible fluorescent protein for fusion tags
title A bright and photostable photoconvertible fluorescent protein for fusion tags
title_full A bright and photostable photoconvertible fluorescent protein for fusion tags
title_fullStr A bright and photostable photoconvertible fluorescent protein for fusion tags
title_full_unstemmed A bright and photostable photoconvertible fluorescent protein for fusion tags
title_short A bright and photostable photoconvertible fluorescent protein for fusion tags
title_sort bright and photostable photoconvertible fluorescent protein for fusion tags
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2745648/
https://www.ncbi.nlm.nih.gov/pubmed/19169260
http://dx.doi.org/10.1038/nmeth.1296
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