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The second osmotic virial coefficient, B 22 , of protein solutions is a function of the protein interaction potentials and, thus, summarizes many solution parameters leading to crystallization or precipitation of proteins. B 22 of hen egg‐white lysozyme and bovine serum albumin was measured by static light scattering under the variation of pH, temperature, and crystallization agents. Comparing B 22 values and precipitate morphology in a systematically analyzed range of solution conditions allows the construction of the so‐called crystallization slot. The thermodynamic driving force for crystallization is supersaturation, which is set by the protein concentration and the solubility (related to B 22 ). Hence, besides the optimal B 22 range, the protein concentration and, if solubilities are available, the supersaturation leads to a two‐dimensional crystallization window where crystal formation is possible. This is shown in a generalized state diagram, where protein morphologies are solely determined as a function of protein concentration or supersaturation and interactions.
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Wanka et al. (2011) studied this question.
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