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The article focuses on optimum solubility screening, an efficient method to optimize buffer conditions for homogeneity and crystallization of proteins. 24 different buffers ranging from pH 3 to pH 10 are screened using a vapor-diffusion method and very small amounts of protein. The solubility of the protein is first determined by visual examination using a light microscope and those drops that remain clear after 24 hour are further evaluated using dynamic light scattering. The ease of use of this screen and the capability of testing many conditions makes this a very efficient means of searching for the best solvent condition for a particular protein.