Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
