Several pieces of equipment in this facility provide an integrated set of different biophysical approaches for studies of macromolecular structure and interactions. The below instrumentation is available as of April 2016.

For further information, please contact Diane Beckford at diane.beckford@asrc.cuny.edu or at 212-413-3221.

  • Microscale Thermophoresis: NanoTemper Monolith NT.115

    This instrument uses changes in thermophoretic mobility – the migration of macromolecules into or away from a zone with elevated temperature – to characterize binding reactions. Advantages of this instrument include low sample consumption (ca. 100 microliters of low micromolar protein samples) and speed of measurement (under one hour for 16 point titration curve).

  • Multiangle Light Scattering (MALS): Wyatt MiniDawn TREOS and OPTILAB REX

    Provides independent measurements of molar mass and size of macromolecules in solution, particularly when coupled with Superdex 75 or Superdex 200 gel filtration chromatography (SEC-MALS).

  • Circular dichroism and fluorescence: Jasco J-1500

    Utilized for studies of protein secondary and tertiary structure, this spectrometer can detect changes in either circular dichroism (monitoring protein backbone environments) or fluorescence (monitoring Trp sidechains and other fluorescent groups). Accessories allow variable temperature operation, automated titrations and stopped-flow experiments.