Calypso CG-MALS Instrument for Characterizing Biomolecular Interactions by Wyatt Technology

Calypso Composition-Gradient Multi-Angle Light Scattering (CG-MALS) instrument from Wyatt Technology characterizes many different macromolecular interactions by using a string of un-fractionated samples of various concentration or composition. It does not require any special modifications such as sample tagging or immobilization procedures. Samples are entirely in solution without any labeling.

Key Features

The following are the key features of the Calypso CG-MALS instrument:

  • Calypso's automation optimizes throughput
  • Calypso software provides a wide choice of interaction models
  • Provides fast and accurate results

The Calypso hardware and software supports the analysis of:

  • Refractive index increment: dn/dc
  • Zimm plots: concentration gradients for measuring solution-average molar mass MW, size Rg, and second viral coefficients
  • Stop flow kinetics: aggregation, dissociation and other time-dependent reactions (equilibration time from seconds to hours)
  • Self- and cross-virial coefficients
  • Non-specific macromolecular interactions
  • Self and/or heteroassociations
  • Absolute molecular stoichiometry of associating complexes
  • KD (equilibrium dissociation constant) from picomolars to millimolars
  • Specific binding and complex assemblies of proteins
  • Dynamic equilibria


The Calypso CG-MALS Instrument is used in the following applications:

  • Biotech R&D – Characterization of macromolecular binding affinity and related complex stoichiometry over a broad range of buffer compositions, temperature scales and time.
  • Drug Discovery – Quantification of binding affinity and stoichiometry of enzyme/inhibitor or antibody/antigen interactions, and the analysis of the influence of tiny molecules on protein-protein interactions.
  • Self-assembly/Aggregation – Measuring the effect of solvent pH, ionic strength, or excipients on polymerization or protein associations and quantifying kinetics of self-assembly and aggregation through rate of change of molar mass and radius of gyration.
  • Process Improvement – Calculating second virial coefficient and fine tuning parameters to optimize formulation stability and viscosity, and determining cross virial coefficients to improve antibody purification and gain insights into the impact of large excipients on formulations.
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