Dear All,
Recently I posted a question about protein induced protein precipitation.
Firstly I'd like to thank many folks for their good ideas.
Later on I did a titration experiment with one protein concentration
fixed at 0.4mg/ml(about 10uM). Now it is clear that these two proteins
stoichiometrically precipitated when they formed a 1:1 complex. The excess of
individual proteins was just soluble in the buffer.
How come these two proteins co-precipitated when they formed a complex?
Does anyone know some methods to keep the complex soluble enough for
crystallization?
By the way, there is some additional information about the individual
components. One has a pI of 6.5, and the other has a pI of 10.
Any suggestions will be highly appreciated.
Jerry McCully
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