Quantitative assessment of fluorescent proteins

Paula J. Cranfill, Brittney R. Sell, Michelle A. Baird, John R. Allen, Zeno Lavagnino, H. Martijn De Gruiter, Gert Jan Kremers, Michael W. Davidson, Alessandro Ustione, David W. Piston

Research output: Contribution to journalArticle

169 Scopus citations

Abstract

The advent of fluorescent proteins (FPs) for genetic labeling of molecules and cells has revolutionized fluorescence microscopy. Genetic manipulations have created a vast array of bright and stable FPs spanning blue to red spectral regions. Common to autofluorescent FPs is their tight β-barrel structure, which provides the rigidity and chemical environment needed for effectual fluorescence. Despite the common structure, each FP has unique properties. Thus, there is no single 'best' FP for every circumstance, and each FP has advantages and disadvantages. To guide decisions about which FP is right for a given application, we have quantitatively characterized the brightness, photostability, pH stability and monomeric properties of more than 40 FPs to enable straightforward and direct comparison between them. We focus on popular and/or top-performing FPs in each spectral region.

Original languageEnglish
Pages (from-to)557-562
Number of pages6
JournalNature Methods
Volume13
Issue number7
DOIs
StatePublished - Jun 29 2016

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    Cranfill, P. J., Sell, B. R., Baird, M. A., Allen, J. R., Lavagnino, Z., De Gruiter, H. M., Kremers, G. J., Davidson, M. W., Ustione, A., & Piston, D. W. (2016). Quantitative assessment of fluorescent proteins. Nature Methods, 13(7), 557-562. https://doi.org/10.1038/nmeth.3891