The present study investigates shape properties of the enzyme dUTPase from Escherichia coli in the solution phase. In this work small angle neutron scattering (SANS) findings on dUTPase/D2O solutions for temperature values of T = 8 °C and T = 37 °C are presented. The analysis of SANS data, carried out by using a prolate ellipsoid core/shell model fitting and the well‐known Guinier and Zimm analysis procedures allows the characterization of the shape of the protein in solution. By means of the comparison with experimental and theoretical data existing in literature on dUTPase in the crystalline state, we find that the protein in solution maintains its dimensions before the denaturation process. Furthermore, by analyzing the SANS spectra of dUTPase/D2O/trehalose solutions, we emphasize the bioprotective effects of trehalose on the protein.Structure of dUTPase.magnified imageStructure of dUTPase.