Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

Near-infrared STED nanoscopy with an engineered bacterial phytochrome.

MPG-Autoren
/persons/resource/persons208316

Kamper,  M.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons79571

Ta,  H.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons128160

Jensen,  N. A.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15210

Hell,  S. W.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15269

Jakobs,  S.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

Externe Ressourcen
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Kamper, M., Ta, H., Jensen, N. A., Hell, S. W., & Jakobs, S. (2018). Near-infrared STED nanoscopy with an engineered bacterial phytochrome. Nature Communications, 9(4762), 1-7. doi:10.1038/s41467-018-07246-2.


Zitierlink: https://hdl.handle.net/21.11116/0000-0002-8067-9
Zusammenfassung
The near infrared (NIR) optical window between the cutoff for hemoglobin absorption at 650 nm and the onset of increased water absorption at 900 nm is an attractive, yet largely unexplored, spectral regime for diffraction-unlimited super-resolution fluorescence microscopy (nanoscopy). We developed the NIR fluorescent protein SNIFP, a bright and photostable bacteriophytochrome, and demonstrate its use as a fusion tag in live-cell microscopy and STED nanoscopy. We further demonstrate dual color red-confocal/NIR-STED imaging by co-expressing SNIFP with a conventional red fluorescent protein.