The Calypso® interfaces with a Wyatt multi-angle light-scattering detector (DAWN® or miniDAWN®) and a UV or RI concentration detector to analyze biomolecular interactions, without labeling or immobilization. The Calypso system determines affinity, absolute molecular stoichiometry of complexes, and the kinetics of self-assembly, aggregation or dissociation of macromolecular complexes, by means of composition-gradient multi-angle light scattering (CG-MALS).
The CALYPSO™ software for control, data acquisition and analysis offers a comprehensive suite of association models for studying self-association and hetero-association including high-order oligomerization, simultaneous self- and hetero-association, and multi-valent interactions. This unique technology nicely complements surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), and other biophysical techniques for characterizing interactions; in addition, it is much faster and simpler than analytical ultracentrifugation.
- Range of Kd: sub-pM to mM, depending on molar mass of the analytes
- Sample requirement: depends on molar mass and Kd. A typical interaction analysis in the range of 1 – 100 nM for ~ 100 kDa proteins requires ~ 100 µg of each protein.
- Solvent compatibility: compatible with most aqueous solvents and alcohols
- Supports automated pre- and post-experiment cleaning cycles
- Software: CALYPSO CG-MALS software controls the Calypso composition gradient system, collects and analyzes MALS and concentration data, and performs fitting to a versatile and customizable range of association models to determine equilibrium dissociation constants Kd, absolute stoichiometry, cooperativity, self-and cross-virial coefficients and kinetics rates. Simulation capabilities help design CG-MALS methods. The software may also be used with manual, cuvette-based light-scattering measurements in a DAWN® or DynaPro® NanoStar®.