Abstract
High-accuracy X-ray diffraction measurements of protein crystals are an important process to determine three-dimensional structures. Investigators must manipulate crystals in X-ray diffraction measurement. Protein crystals are exposed to evaporation during manipulation, and their exposure to evaporation for a long time causes serious damage. Recently, we have developed a novel technique of protein crystallization using a semi-solid agarose gel (SSAG), which demonstrated several desirable merits such as the growth of crystals with high quality, growth with a high nucleation rate, and the possibility of automated crystal capture. To further assess the merits of SSAG-grown crystals, we evaluated the effects of evaporation on the quality of SSAG-grown crystals using X-ray diffraction and subsequent structural analyses. The results demonstrate that the SSAG-grown crystals showed a high tolerance to evaporation, compared with the solution-grown crystals. These comparative experiments also demonstrate the practical advantages of efficient protection by the SSAG surrounding the protein crystals.
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