Hi Guohui, Instead of truncation, have you considered mutating some or all of the cysteine residues in the N-terminus? When we did our HAV 3C study, we had to change a surface Cys to serine (evidence of intermolecular disulfide linkage); the resultant variant not only stayed monomeric for longer time, but it also proved much easier to crystalize.
Best, Jiang On Tuesday, September 15, 2020, Guohui SHANG <sz20183020...@cau.edu.cn> wrote: > Hi Everyone， > Well,My Research Protein is easily Dimerzation caused by Disulfide bond for many Cys.And it leads to the SEC peak too wide about 5 mL. Then I Cut N-ter 30 Amino Acids in which 5 spaced Cys,but the SEC Peak is still wide and hard to Crystallize（as the protein is very pure and clean）.Besides, I have tried different Buffer pH ＜ pI or pH ＞ pI，but the SEC peak Do not Work at all. > Anyone could offer your kindly ideas,I would thank you very much！ > ________________________________ > 发自我的iPhone > ________________________________ > > To unsubscribe from the CCP4BB list, click the following link: > https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 -- Jiang Yin, Ph.D. Department of Biochemistry University of Alberta Edmonton, AB T6G 2H7 Canada 780-4920610 ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
