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Abstract
The translational diffusion coefficient of bovine pancreatic ribonuclease A, a globular protein, has been measured by dynamic light scattering under various conditions related to the crystallization process. In all cases, a monomodal light scattering autocorrelation function was observed. The diffusion coefficient exhibited a linear dependence on protein concentration and an interaction parameter could be calculated. Attractive interactions were found to increase with salt concentration and to decrease with pH in the presence of salts. Finally, optimal crystallization conditions correspond to moderate attractive interactions.
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