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Dynapro ms x dls instrument

Manufactured by Wyatt Technology
Sourced in United States

The DynaPro MS-X DLS instrument is a dynamic light scattering (DLS) instrument designed for the characterization of macromolecules and nanoparticles in solution. The instrument measures the hydrodynamic size, size distribution, and polydispersity of samples using the principles of DLS.

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2 protocols using dynapro ms x dls instrument

1

Protein Characterization by DLS and Light Scattering

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Dynamic light scattering (DLS) was measured with a DynaPro MS-X DLS instrument (Wyatt, Santa Barbara, CA, USA). Dynamics v6 software (Wyatt Technology Corporation, Santa Barbara, CA, USA) was used for data collection and processing. Sets of DLS data were measured at 15 μM and 25 °C unless stated specifically, with an average of 50 acquisitions and an acquisition time of 10 s.
Static scattering intensities were measured with a DynaPro MS-X DLS instrument (Wyatt, Santa Barbara, CA) or a Malvern μV instrument (Malvern Panalytical, Malvern, UK) at 25 °C in 50 mM sodium phosphate buffer (pH 7.4) at varying protein concentrations in the range of 0.2–4.5 g L−1. The intensities were analyzed using a Debye plot as represented by Equation (1)
K·c/R90=1/Mw+2A2c
which is valid for particles significantly smaller than the wavelength of the incident radiation, where K is the optical constant of the instrument, c is the particle mass concentration, R90 is the Rayleigh ratio of scattered to incident light intensity, Mw is the weight-averaged molar mass, A2 is the 2nd virial coefficient that is representative of interparticle interaction strength and Mw can be determined according to the intercept of the plot.
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2

Measuring Protein Hydrodynamic Radii and Molar Mass

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The apparent hydrodynamic radii of the proteins were measured using dynamic light scattering (DLS) in a DynaPro MS-X DLS instrument (Wyatt, Santa Barbara, CA, USA). Dynamics v6 software (Wyatt Technology Corporation, Santa Barbara, CA, USA) was used in data collection and processing. Sets of DLS data were measured at 25 °C with an average number of 50 acquisitions and an acquisition time of 10 s. Measurements were carried out in 50 mM sodium phosphate buffer pH 7.4 and 50 mM glycine/HCl buffer pH 2.5.
Static scattering intensities were measured in a Malvern μV instrument (Malvern Panalytical, Malvern, UK) at 25 °C, in 50 mM sodium phosphate buffer pH 7.4, at different concentrations of protein in a range of 0.2 to 3.5 mg mL−1. The intensities were analyzed using the Debye plot as represented by Equation (1),

valid for particles significantly smaller than the wavelength of the incident radiation, where the K is an optical constant of the instrument, c is the particle mass concentration, R90 is the Rayleigh ratio of scattered to incident light intensity, Mw is the weight-averaged molar mass, and A2 is the 2nd virial coefficient that is representative of inter-particle interaction strength. Mw can be determined from the intercept of the plot.
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