Lee leads TheLeeLab at Cambridge Chemistry, focused on developing cutting-edge biophysical single-molecule fluorescence methods to answer fundamental biological questions. Two major thrusts: (1) 3D super-resolution microscopy instrument development — the lab pioneered single-molecule light field microscopy (SMLFM) using a microlens array in the back focal plane, achieving ~10× speed improvement over double-helix PSF for volumetric imaging; also develops vortex light field microscopy (VLFM) for simultaneous 25 nm spatial / 3 nm spectral precision; (2) Biological applications — studying T-cell receptor signalling at the nanoscale (distribution of TCRs, microvilli-mediated close contacts), histone assembly during DNA replication and repair in fission yeast, and PSD-95 nanoclusters in mouse brain using 3D SMLM. A job posting (PDRA) was active in 2025 for T-cell imaging work with super-resolution and Fourier light-field microscopy.
Natrajan's group develops luminescent lanthanide complexes for chemical and biological sensing. Research directions: (1) Time-gated lanthanide luminescence sensing — long-lifetime Eu3+, Tb3+, and Yb3+ complexes with millisecond emission lifetimes for background-free sensing in cells and tissue; (2) Intracellular sensing — luminescent probes for sensing O2, pH, viscosity, and specific enzymes inside living cells with spatiotemporal resolution; (3) Chiral discrimination — circularly polarized luminescence (CPL) from Eu3+ complexes for enantioselective sensing; (4) Responsive probes — switchable lanthanide complexes as ratiometric sensors for biomedical imaging. The long-lifetime emission enables time-gating strategies analogous to quantum sensing protocols.
Olaya-Castro leads theoretical research on quantum phenomena in biological systems. Research directions: (1) Quantum coherence in photosynthesis — open quantum systems theory for energy transfer in light-harvesting complexes, probing whether quantum coherence provides functional advantage; vibronic coupling models for chromophore-protein complexes; (2) Counting statistics and noise in exciton and charge transfer; (3) Quantum thermodynamics of biomolecular machines — efficiency limits and entropy production in molecular motors; (4) Non-classical features of electronic/vibrational dynamics in chromophores; (5) Connections between quantum information measures and biological function. Collaborates with Bain and Llorente-Garcia on joint experiment/theory biosensing projects. Theoretical work only — no experimental activity.
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.
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.
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.
Vafabakhsh uses single-molecule FRET to resolve the conformational dynamics of membrane receptors and channels -- including class C GPCRs, adhesion GPCRs, and potassium channels -- as they gate and signal, and applies related single-molecule methods to viral DNA packaging motors and synaptic protein complexes, aiming to build a quantitative, multi-scale picture of synaptic protein organization from the single-molecule to the synapse level.