Hey Rakesh, Such are the questions that every crystallographer faces in his/her everyday life. I am not sure if there is any straight forward answer. So make voyages ! Terese Bergfors mentioned in her famous book, "Protein crystallization" a case where a Scientist from Umea Uni got the diffraction-quality crystals only by changing the reducing agent in the protein buffer. Now who could have guessed that :)
Best wishes -Z Zaigham M Khan, PhD Associate Scientist Icahn School of Medicine at Mount Sinai Department of Oncological Sciences 1470 Madison Avenue New York United States On Tue, Jul 27, 2021 at 11:55 AM Rakesh Chatterjee <rakesh.2665...@gmail.com> wrote: > Hi everyone > > I was working on a protein complex where one protein binds with the other > protein majorly based on its surface charge. The protein complex yields > nice crystals but does not diffract. Additionally the crystals used to > dissolve within the drop when allowed for incubation both at 18 degrees and > 4 degrees. Repeated rMMS microseeding, construct variations and changes in > purification strategies did not yield any diffractions. Conditions involved > for the protein complexes primarily involved PEG with various > strengths and pH variations. Looking for your suggestions and valuable ideas > > Thanks in advance > Dr Rakesh Chatterjee > Umea University > Umea Sweden > > > ------------------------------ > > To unsubscribe from the CCP4BB list, click the following link: > https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 > ######################################################################## 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/
