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Dear CCP4er,
I have an interesting observation for one of my DNA binding protein--when the
length of DNA flanking both DNA binding site increase, the solubility of
protein-DNA complex increases. And I can get a nice sigmoid curve from protein
solubility versus DNA length. The solubility of prot
t to binding DNA and finally
purify with gel filtration column. However, the one I am currently working
on seems to be very picky. If you have any suggestion regarding to my
problems, I will be thankful.
Best regards,
--
Wei Huang, PhD
Postdoctoral Associate
Center for Proteomics and Bioinformatics
Dear CCP4ers,
I am working on purifying a protein-DNA complex for structural and
biochemical studies. So far, I can readily make protein > 95% pure in high
salt buffer. However, I have some problems in assembling the protein-DNA
complex.
1) My protein precipitates at low salt buffer. I think this