Many proteins are stored as frozen solutions or in amorphous solid (lyophilized) phases to minimize chemical and physical degradation during their shelf life. Different pharmaceutical formulations are developed to avoid protein degradation and irreversible aggregation during freeze-drying (lyophilization) and storage. Polyhydroxy compounds, including carbohydrates (sugars) and sugar-alcohols, are well-known cryo and lyo-protectors that can minimize destabilization of proteins during the freeze-drying processes. However, freeze-destabilization of proteins is commonly observed even in the presence of these components. In our previous study we investigated the influence of sorbitol as a cryo-protector by employing in situ SANS technique to detect protein crowding, phase separation and large-scale heterogeneity in frozen solution model systems. The current proposal is aimed to extend these studies to the common pharmaceutical lyoprotectors (i.e, sugars) and a model protein, BSA, which is commonly used to mimics aggregation behavior of typical pharmaceutical proteins.