Rueda leads a single-molecule imaging group (jointly at Imperial and the MRC London Institute of Medical Sciences) that combines single-molecule FRET, fluorogenic RNA aptamer imaging and optical tweezers to reveal the structural dynamics of RNA folding/splicing, CRISPR-Cas9 target search and off-target activity, and chromatin-remodelling complexes; the aptamer-imaging technology has been spun out as the startup Irida.

Applies advanced single-molecule biosensing to study the cyanobacterial circadian clock — the only fully reconstitutable in vitro biochemical oscillator. Directions: (1) single-molecule FRET and fluorescence imaging to track conformational states of KaiC ATPase during clock cycles with single-protein resolution; (2) single-molecule reconstitution of the complete KaiA/KaiB/KaiC oscillator; (3) mathematical modeling of biochemical oscillation. Technique focus: single-molecule fluorescence as quantitative biosensing tool for protein conformational dynamics. Joint appointment Microbiology.

Uses single-molecule spectroscopy, optical trapping, and advanced imaging to study nanoscale systems. Directions: (1) orientation-resolved single-molecule spectroscopy using polarization-controlled excitation and detection; (2) optical trapping of individual nanoparticles and viruses to study force-dependent dynamics; (3) plasmon-enhanced single-molecule detection and imaging beyond diffraction limit; (4) ultrafast spectroscopy of nanoscale energy transfer.

Schueder is a newly appointed (2025) EPFL Assistant Professor specializing in high-resolution microscopy and its biological applications. He played a key role in the development of DNA-PAINT, a super-resolution microscopy technique enabling nanometer-scale (~5 nm) visualization of cellular structures via transient programmable DNA hybridization. Research directions: (1) DNA-PAINT super-resolution — multiplexed, quantitative imaging of protein complexes in fixed and living cells with Exchange-PAINT; (2) Single-molecule localization below 5 nm resolution — resolving individual proteins within complexes; (3) Biological applications — imaging cytoskeletal networks, receptor clustering, chromatin organization; (4) Expanding to in situ structural biology — correlating super-resolution images with cryo-EM data. Transferred from ETH Zurich. Strong fit with EPFL imaging and structural biology ecosystem.

Develops and applies single-molecule fluorescence super-resolution imaging (including FIONA, nanometer-accuracy localization) to study the structure and dynamics of molecular motors (myosins, kinesins, dyneins) and other biological macromolecules.

Shaevitz combines custom super-resolution and multifocal/3D imaging instrumentation with single-molecule tracking to make precision measurements of bacterial cell-shape mechanics, cytoskeletal dynamics (e.g. MreB), collective motility and pattern formation, and animal behavior quantification. His lab pioneered 3D live-cell imaging of bacterial shape during growth and continues to develop chromatic multifocal and localization-microscopy instrumentation in collaboration with the Yang and Gregor labs.

Sierecki co-developed the cell-free single-molecule interaction platform with Gambin and runs a group applying it to protein interaction networks: mapping which proteins bind which, with what affinity and in what stoichiometry, at throughput high enough to screen rather than characterise one pair at a time. Recent applications include viral protein-host interactions and transcription factor complexes. Positioned against the established body of NV-ensemble quantum sensing work — DEER, nanoscale NMR and T1 relaxometry protocols operating at pT/sqrt(Hz) field sensitivity — the relevance to a quantum-sensing candidate is as a source of well-characterised, quantitatively-defined biological targets: a pT/sqrt(Hz)-class sensor is only useful in biology if someone can tell you exactly what molecular species is present and at what concentration, which is what this platform delivers. Borderline inclusion — no quantum or physics-instrumentation component — kept because single-molecule technique development is the core of the group.

Smith runs Melbourne's time-resolved fluorescence facility and specialises in the information channels most people throw away: fluorescence lifetime, anisotropy decay and its orientational content, and single-molecule photophysics, applied to organic semiconductors, energy-transfer systems and biological samples. The group builds its own confocal microspectroscopy instrumentation for time-resolved anisotropy imaging and single-molecule detection. Positioned against the established body of NV-ensemble quantum sensing work — DEER, nanoscale NMR and T1 relaxometry protocols operating at pT/sqrt(Hz) field sensitivity — lifetime- and orientation-resolved fluorescence is the principal orthogonal contrast mechanism to spin-based sensing, and his instrumentation is the natural correlative partner for NV-ensemble DEER/relaxometry experiments at pT/sqrt(Hz) that need an independent optical readout of the same specimen. Preferred attribute present: orientation- and lifetime-resolved methods.

Research centers on manipulating and measuring single molecules with quantum-level precision. Primary platform: ABEL trap (Anti-Brownian ELectrokinetic trap) for single-molecule confinement in free solution without surface tethering, enabling measurement of spectroscopic identity, molecular dynamics, and nanoscale energy transfer at femtomolar concentrations. Also develops orientation-resolved single-molecule imaging and single-molecule FRET for photoadaptation in photosynthetic systems and nanoscale immune cell signaling. QuBBE member. PhD Physics UChicago; joined 2024.

Uses ultrafast multidimensional spectroscopy to study structural dynamics of biomolecules. Directions: (1) 2D IR spectroscopy of protein folding, water dynamics, and membrane systems with sub-100-fs time resolution; (2) single-molecule FRET for resolving conformational heterogeneity in proteins and nucleic acids; (3) development of ultrafast mid-IR laser sources and pulse shaping for 2D spectroscopy. Resolves dynamics inaccessible to other methods.