Abstract: Biomolecular crystallography strives to explore the appropriate growth conditions leading to diffraction quality crystals for structure determination. Various commercially available crystal screens are often used to search for optimum crystallization conditions. These screens consist of combinations of buffers, salts, precipitant and additives resulting in a large number of possible combinations of crystallization conditions. Increasing the solubility of the protein in its buffer to an optimum level favors crystallization over precipitation. A recent study determined that using solution conditions which enhanced protein solubility lead to better quality crystals in most cases examined. An enhancement in the solubility lowers the attractive forces between the protein molecules and crystal-liquid interfacial tension. This lowers the energetic barrier to nucleation of protein crystals as determined through nucleation kinetic data. Excessive enhancement in the solubility may lead to the near elimination of the barrier thus leading to precipitation. This work focuses on analyzing the effect of various solubility enhancers on the crystallization of selected proteins. The use of organic solvents such as ethanol, ethylene glycol, glycerol and 2-methyl-2,4-pentane diol as solubility enhancers for selected proteins in their optimized buffer conditions is evaluated.