The H-Ras protein is a GTPase important to cell cycle and differentiation. Mutations in this protein have been associated with 30% of cancers. A better understanding of this protein could lead to innovative treatments of cancers caused by the mutations. Solvent mapping of the crystallized Q61L mutant of the H-Ras protein with glycerol shows with potential areas of protein⁄protein interactions, areas that are of particular interest in the design of anti-cancer drugs. This study investigated whether glycerol can distinguish changes in the surface due to the mutation. A comparison was made between the wild-type and Q61L mutant H-Ras crystal structures in glycerol and aqueous solution. The structural analysis lead to the conclusion that the main changes observed were due to the solvent environment and not to the mutation.