A novel approach to the solubility measurement of protein crystals by two-beam interferometry

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Abstract A novel technique was developed for the rapid solubility measurement of protein crystals (lysozyme) by two-beam interferometry. The merits of this technique are: (1) time saving (less than 2 h to obtain one experimental point), (2) the small amount of the sample (∼66 μl), (3) high accuracy, (4) applicable to the solubility measurement of a metastable phase and (5) insensitive to impurities. The limitations of the present technique are also discussed.

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