🥳I'm excited to share our recent work on automated, single-molecule data analysis suitable for multi-labeled structures, called Deep-LASI! Congrats to all authors and thanks for this great collaboration between the Lamb group and @LabTinnefeld!
https://t.co/88WO1uF7Sl
Read the full story here: https://t.co/a3E6bOIPJB
This project received funding from the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie Grant agreement no. 101029907.
6/6
A side-project that evolved into a quite detailed exploration of zero-mode waveguide ‘nanowells’ for in vitro and in vivo (!) fluorescence microscopy.
Now out in @acsnano:
https://t.co/a3E6bOIPJB
Many thanks to @_SoraY and @MarvinTanenbaum for the nice collaboration!
1/6
This was put into practice by @_SoraY who successfully grew cells on the palladium surface.
Even in the presence of micromolar cytoplasmic background signal (too high for TIRF), we could resolve the signal of single membrane-bound proteins diffusing within the ZMW nanowells.
5/6
Latest #CDlab paper now online in @acsnano: https://t.co/GPKizeyFll
In collaboration with @MarvinTanenbaum's lab we developed zero-mode waveguides for detection of single molecules within live cells that protrude into the cavity.
1/
Come work with us! We are recruiting a 2-yr postdoc/research fellow for an exciting project using single-molecule microscopy to study viral replication. closing date 17th Sept. More info & how to apply here: https://t.co/geuqp1WK4Z
@LipfertLab @KukuraLab @RunningPhoton I can at least confirm that (in our hands) calibration curves for protein and DNA ladders seem to coincide in terms of mass.
The main paper of my PhD, our smFRET study of sub-millisecond structural dynamics in A2A adenosine receptor (GPCR) is out in @CommsBio ! 🥳🥳🥳
https://t.co/BhHgtNnBHy
After two years from #preprint to publication I have no words
Sisyphus turned into Heracles, finally!
Five years later we have a really strong follow-up study to this one (https://t.co/96w8GgJiuV) showing that smFRET data are reproducible enough to be trusted for dynamic structural biology applications of proteins.
An multi-lab, blind study confirms that smFRET measurements on dynamic proteins are highly reproducible across instruments, analysis procedures and timescales, further highlighting the promise of smFRET for dynamic structural biology. https://t.co/EIPBxapRbG
The single-molecule #FRETcommunity seems to love international benchmark studies... so here is the newest one!
We tested the reproducibility of smFRET experiments on highly dynamic protein systems.
Spoiler: It still works remarkably well!
https://t.co/PtZmXgU4y1
@naturemethods
Instead of a lengthy Tweetorial, first author Ganesh and I wrote a short summary of the paper, including our personal experiences along the way.
Read it here: https://t.co/KRJNMtsBr3
@ganesh__agam