Aggregates of the globular protein beta-lactoglobulin were formed by heating solutions of native proteins at pH 7, after which gels were formed by the addition of salt. The second step does not necessitate elevated temperatures and is therefore often called cold gelation. The structure of the gels was studied during their formation using light scattering and turbidity. Complementary confocal laser scanning microscopy measurements were done. We compared the structure with that of gels formed by heating native beta-lactoglobulin under the same conditions. Whereas in the latter case, microphase separation occurs above 0.2 M NaCl, no microphase separation was observed during cold gelation up to at least 1 M NaCl. The dependence of the kinetics and the final gel structure on the protein concentration, the temperature, the salt concentration, and the aggregate size was quantified. A few measurements on gels formed by adding CaCl2 confirmed the higher efficiency of this bivalent cation but revealed no qualitative differences with gels formed by adding NaCl.