I have purified protein using affinity and ion exchange, in both of the buffers i used ph of 7.9, while concentrating in buffer exchange, i changed the ph to 7.5 and concentrated upto 5.4 mg/ml and set up for crystallization. will the change in ph affect the crystallization process ? my protein ideal ph is 7.4
Yes for have Nucleation zone and Metastase zone you can adjust parameters include precipitant or additive concentration, pH and temperature. If you observe a clear solution (undersaturation) after crystallisation screening you can try by increasing protein concentration (10mg/ml or 20mg/mL).
It's not clear what your question is. Do you have any results for the other pH such that you expect a change in the lower pH? If not, there is no way to predict how the pH in your protein solution will affect the crystallization. Even more so without knowing the concentration of your buffer, since you usually mix the protein solution with the crystal screen buffers leading to a variable final pH over a wide range. Last not least, what does "ideal pH of 7.4" for your protein mean? Highest stability, best crystallization condition or do you mean the pI of your protein?
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