Benjamin Ambrose

TL;DR: A multi-laboratory study finds that single-molecule FRET is a reproducible and reliable approach for determining accurate distances in dye-labeled DNA duplexes.

TL;DR: The state-of-the-art in single-molecule FRET (smFRET) has become a mainstream technique for studying biomolecular structural dynamics as mentioned in this paper, which has generated significant progress in sample preparation, measurement procedures, data analysis, algorithms and documentation.

TL;DR: The smfBox is presented, a cost-effective confocal smFRET platform, providing detailed build instructions, open-source acquisition software, and full validation, thereby democratisingSmFRET for the wider scientific community.

TL;DR: In this paper , an international blind study involving 19 laboratories was performed to assess the uncertainty of FRET experiments for proteins with respect to the measured FRET efficiency histograms, determination of distances, and the detection and quantification of structural dynamics.

TL;DR: The addition of divalent metal ions to the active site of the hFEN1–DNA substrate complex demonstrates that active site changes are propagated via DNA-mediated allostery to regions key to substrate differentiation.