Protein Crystallography and Biophysics Centre (BiophysX)
Institute of Structural and Molecular Biology (ISMB)
Birkbeck College / University College London

Fluorescence (Fluoromax-3)

Fluorescence changes are caused by electronic changes in the vicinity of the fluorophore. Depending on experimental design, fluorescence intensity changes can therefore give information on macromolecular conformational changes, oligomerisation, ligand binding, solvent accessibility and similar questions. Fluorescence anisotropy (polarization) changes with the mobility of the fluorophore and therefore the size of the molecule it is part of. Anisotropy works even if there is no intentisy change.

The Fluoromax-3 (Horiba Jobin Yvon) at the ISMB BiophysX Centre is a highly accurate and versatile fluorescence spectrophotometer with excitation as well as emission monochromators and polarizers. The Micromax-384 plate reader can be connected and used for intensity measurements.

Fluorescence experiment possibilities:
-    excitation and emission spectra
-    combined excitation/emission scans (discovery scans)
-    single wavelength analysis
-    time-based fluorescence measurements (time courses, slow kinetics)
-    anisotropy (polarization)

Sample requirements
  • Cuvettes: 100 μl 0 3 ml quarz, stirring is possible with some of them.

  • Sample changer for four samples in parallel measurement.

  • Microplate reader Micomax for 4x6, 8x12, 16x24 well plates (24,96,384) for extensive screening projects.

  • Temperature range: 4 - 85oC


Please contact us for detailed protocols and planning your experiment.

ISMB Protein Crystallography and Biophysics Centre, Birkbeck, University of London
Last modified April 2021