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

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