Monitoring protein crystallization by dynamic light scattering
Crystallization of lysozymes induced by temperature lowering has been monitored by dynamic light scattering from the onset of supersaturation to the growth of protein crystals up to a noticeable size (150–200 μm). The apparent size of the scatterers was found to increase up to a maximum value as supersaturation proceeded, then to decrease down to its initial value. Apparitions of crystals (20–30 μm) were observed during this decrease. Light scattering is thus proved to be a sensitive technique to follow protein crystallization and to provide useful information on the process.