Growth of protein crystals in high-strength hydrogels with the dialysis membrane

This study focused on protein crystallization in high-strength hydrogels to expand the application of protein crystals. The results of our previous studies demonstrated several desirable merits, such as growth with a high nucleation rate and a high tolerance to solvent evaporation. However, the crystallization method faces the problem of handing protein solutions at high temperatures, which often causes the proteins to become inactivated or aggregated. This study established a new crystallization method that prevents high-temperature damage to proteins. This method offers a technique to osmose the protein from the top of a hydrogel layer and recover its crystals as the precipitant on the bottom of the hydrogel layer by using a handmade plate with a dialysis membrane. This study concentrated on the protein crystallization in hydrogels, but the results indicate that this method will be applicable to various proteins because it can always be operated at a low temperature.

Automated summary

This study introduced a new method for protein crystallization in high-strength hydrogels to prevent protein damage at high temperatures and found that this method is applicable to various proteins due to its low-temperature operation.