The association of hen egg white lysozyme was observed using time-resolved multi-angle static and dynamic light scattering. In solutions containing 1.2M of NaCl with a pH of 4.6 buffered by 50 mM of NaAc, and maintained at 20 degrees C, the apparent molecular weight M-w and gyration radius R-g, of lysozyme aggregates were measured at 0.3-5-s intervals for various lysozyme concentrations from 8 to 32 mg/mL using static light scattering. At 32 mg/mL, liquid-liquid phase separation (LLPS) occurred. The (Kc/Delta R(q))(1/2) vs. q(2) plot had a non-linear shape with a maximum at a particular q(2), indicating that the aggregate size distribution was within a narrow range. This had not been observed in our previous studies of high-molecular-weight proteins. The dynamic light scattering data were consistent with those of static light scattering; i.e., CONTIN analysis showed clear bimodal (monomer and aggregate) distributions. Fractal dimension analysis of the aggregates with the protein concentration showed that the inner structure of the scatterer formed during LLPS was rigid in the final stage, which supports a two-step nucleation model. (c) 2007 Elsevier B.V. All rights reserved.