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Q: Fachverband Quantenoptik und Photonik

Q 65: Nano-Optics and Biophotonics

Q 65.5: Vortrag

Freitag, 9. März 2018, 11:30–11:45, K 0.023

Exploring protein structure with cryogenic optical localization in three dimensions — Daniel Boening, •Franz Ferdinand Wieser, and Vahid Sandoghdar — Max Planck Institute for the Science of Light, Erlangen, Germany

Super-resolution optical microscopy has considerably advanced the study of cellular processes, but optical access to the molecular structure of proteins and biomolecular assemblies remains very limited. We have recently exploited the enhanced photostability of fluorophores at cryogenic temperatures to increase the number of detected photons, thus reaching a significantly higher signal-to-noise ratio compared to room-temperature measurements. Using this approach, cryogenic optical localization in three dimensions (COLD) is capable of determining the positions of several fluorescent sites within a single protein at Angstrom resolution [1]. We present results on imaging DNA Origami, the four binding sites of streptavidin and the conformational state of the Per-ARNT-Sim domain of the histidine kinase CitA. With its high spatial resolution COLD opens new possibilities for obtaining quantitative structure information from small to medium sized biomolecules and for correlative measurements with established imaging methods.

[1] S. Weisenburger et al., Nature Methods 14, 141-144 (2017).