Osmolytes, including sugars and polyols, are well known to suppress denaturation and aggregation of proteins and prevent deactivation of enzymes. Trehalose, a nonreducing disaccharide, is thought to have an excellent stabilizing action. Trehalose is produced by organisms with tolerance to extreme environments. By using synchrotron radiation X-ray wide-angle scattering (WAXS), we have found that trehalose dissociates aggregates of bovine myoglobin denatured by acidic solvents, and then folds it into a native structure. Denaturants and surfactants have been used as additives that dissociate aggregates; however, most of them are cytotoxic. Therefore, this report would suggest that trehalose is a promising candidate as a protein aggregation dissociator that is harmless to the human body. In addition, this study shows the usefulness of the wide-angle scattering method for protein structure analysis in the presence of co-solute.