The translational diffusion coefficient of bovine pancreatic ribonucle
ase A, a globular protein, has been measured by dynamic light scatteri
ng 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 p
rotein concentration and an interaction parameter could be calculated.
Attractive interactions were found to increase with salt concentratio
n and to decrease with pH in the presence of salts. Finally, optimal c
rystallization conditions correspond to moderate attractive interactio
ns.