PUBLICATION
mScarlet: a bright monomeric red fluorescent protein for cellular imaging
- Authors
- Bindels, D.S., Haarbosch, L., van Weeren, L., Postma, M., Wiese, K.E., Mastop, M., Aumonier, S., Gotthard, G., Royant, A., Hink, M.A., Gadella, T.W.
- ID
- ZDB-PUB-161123-14
- Date
- 2017
- Source
- Nature Methods 14(1): 53-56 (Journal)
- Registered Authors
- Keywords
- Cellular imaging, Fluorescent proteins
- MeSH Terms
-
- Cell Survival
- Molecular Imaging/methods*
- Bone Neoplasms/metabolism
- Bone Neoplasms/pathology
- Luminescent Proteins/metabolism*
- Bacteria/metabolism*
- Tumor Cells, Cultured
- Bacterial Proteins/metabolism*
- Humans
- Osteosarcoma/metabolism
- Osteosarcoma/pathology
- HeLa Cells
- Protein Engineering/methods*
- Fluorescence Resonance Energy Transfer/methods*
- PubMed
- 27869816 Full text @ Nat. Methods
Citation
Bindels, D.S., Haarbosch, L., van Weeren, L., Postma, M., Wiese, K.E., Mastop, M., Aumonier, S., Gotthard, G., Royant, A., Hink, M.A., Gadella, T.W. (2017) mScarlet: a bright monomeric red fluorescent protein for cellular imaging. Nature Methods. 14(1):53-56.
Abstract
We report the engineering of mScarlet, a truly monomeric red fluorescent protein with record brightness, quantum yield (70%) and fluorescence lifetime (3.9 ns). We developed mScarlet starting with a consensus synthetic template and using improved spectroscopic screening techniques; mScarlet's crystal structure reveals a planar and rigidified chromophore. mScarlet outperforms existing red Förster proteins as a fusion tag, and it is especially useful as a fluorescence resonance energy transfer (FRET) acceptor in ratiometric imaging.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping