Biophysical Fluorescence Laboratory
Center For Bioimaging Sciences
Departments of Biological Sciences & Chemistry

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Instrumentation

We design, build and refine fluorescence instruments with single-molecule sensitivity, from camera-based imaging FCS to new low-cost platforms, and make them available to other researchers.

Cost-effective dark-field scattering correlation spectroscopy setup, samples and analysis
Setup, samples (gold nanoparticles in solution, on supported lipid bilayers and on cell membranes) and correlation analysis of the dark-field scattering platform.

Dark-field scattering correlation spectroscopy

We developed a cost-effective dark-field scattering correlation spectroscopy platform for quantitative measurement of nanoparticle dynamics. Validated across GNPs in solution, supported lipid bilayers, and cell membranes, the platform enables detection of mobility changes and provides a foundation for antimicrobial screening based on membrane disruption.

Single-molecule binding events

With collaborators, we developed a way to discriminate genuine single-molecule binding events from diffraction-limited fluorescence, extending what can be measured with standard fluorescence microscopes.

Total internal reflection fluorescence microscope used for ITIR-FCS
One of the lab’s total internal reflection fluorescence (TIRF) microscopes used for imaging FCS.

Imaging FCS microscopes

Conventional FCS records one spot at a time. By pairing fast, sensitive EMCCD and sCMOS cameras with illumination that excites only a thin plane of the sample, we record thousands of FCS curves at once and turn them into maps of diffusion and concentration.

We run two total internal reflection (ITIR-FCS) systems, light-sheet (SPIM-FCS) setups for thicker samples and live organisms, and confocal FCS. Full specifications are on the ITIR-FCS, SPIM-FCS and Confocal-FCS pages.

Recent publications

  1. Discriminating single-molecule binding events from diffraction-limited fluorescenceYin Y, Pathoor N, Sharma KK, Zhu S, Long YL, Yan SA, Sim SR, Lin YLY, Wohland T, Wang LNature Communications (2025). doi.org/10.1038/s41467-025-64812-1Single-molecule binding
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