Right on target. Many proteins require some ionic strength in the
solution to maintain solubility and prevent protein aggregation. Usually
NaCl is used for this purpose. You can also use glycerol to enhance
solubility, but this may interfere with crystallization if that's the
next step. NaCl us
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Hello Dhana,
use a buffer at least, and some salt - if I remember correctly, gel
filtration resins require 150mM salt concentration for proper
separation (might have been 50mM). Even 150mM may be too little to
keep your protein soluble.
Best,
Tim
On
On 20 Nov 2013, at 21:56, Dhanasekaran Varudharasu wrote:
> Dear Crystallographers,
>
> I dialysed a 30 kDa protein
> (Recombinant protein which was eluted by 20 mM Tris, 500 mM NaCl, 120 mM
> imidazole) against water for overnight. But it gets precipitat
Dear Crystallographers,
I dialysed a 30 kDa protein
(Recombinant protein which was eluted by 20 mM Tris, 500 mM NaCl, 120 mM
imidazole) against water for overnight. But it gets precipitated after 12
hours. Can anybody give some suggestion to avoid precipitat
