Providing Nanosizing of Particles with the DelsaMax™ Series from Beckman Coulter

The DelsaMax Series from Beckman Coulter are extremely high-speed systems enabling concurrent analysis of zeta potential as well as particle size for small sample volumes of about 45µl, in less than one second.

The benefits of the new DelsaMax™ Series are high accuracy, consistency and speed, allowing nanoparticle research improvement. It is possible to obtain lot of information from even the smallest of samples.

The DelsaMax Series is an addition to a high quality series of sophisticated particle characterization solutions from Beckman Coulter, developed over fifty years back, when Wallace Coulter pioneered the technique that established the field.

Key Specifications

Specifications of the DelsaMax Pro

DelsaMax Pro
Size Range 0.4 to 10,000 nm, hydrodynamic diameter (limited by particle sedimentation)
Molar Mass Range 5×107 g/mol (Da) (dependent on molecular shape model)
Minimum Sample Volume 45 µL
Minimum Measurement Time 1 second
Zeta Potential Measurement
Minimum Sample Volume 170 µL, excluding tubing
Ionic Strength Range 0 to 50 mS/cm (4 times the conductivity of physiological saline)
Mobility Range No practical limit
Mobility Size Range 2 nm to 15 µm diameter
Mobility Sensitivity 1 mg/µL Lysozyme
Minimum Measurement Time 1 second

Specifications of the DelsaMax Core

Size Measurement
Dynamic Light Scattering Size Range (Diameter–nm) 0.4 to 5,000
Static Scattering Molecular Weight Range 300 to 106 Da (concentration dependent)
Minimum Sensitivity 0.1 mg/µL Lysozyme
Scattering Angle 90°
Minimum Sample Volume 1.25 µl standard cuvette, 4 µl disposable cuvette
Correlator 512 channels (100 nsec sampling time in a multi-tau layout)
Data Acquisition Time 1 to 3,600 seconds
Minimum Measurement Time 1 second

Key Features

The key features of the DelsaMax™ Series are:

  • Two concurrent detection systems allow fast measurements
  • Offers 32 simultaneous measurements considerably minimizing run time and improving accuracy
  • With both real and dynamic static light scattering, ten protein measurements can be obtained without sample degradation
  • Instant cross-checking of results is possible with parallel independent measuring systems
  • Proprietary normalization algorithm offers suitable distributions
  • The particles of interest are selected by the optimized auto-correlation function
  • Without re-running of samples, datapoints or flyers can be edited
  • Results can be easily overlaid to verify consistency and accuracy

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