> (20g/l is what I was taught to be the average starting concentration for
crystallisation experiment
I think this needs to be seen in context of each protein. The idea is to get
as close as reasonable (w/o danger of premature precipitation) to the
particular protein's solubility limit. That can be very low, and values in
or below the mg/ml range have been reported. On the other hand, a secreted
plasmaprotein or so may go to much higher values. So, I venture that we are
dealing with a highly skewed and broad parent distribution, and the average
- as precise it may appear - is a) biased towards the large fraction of
garden-variety stuff deposited so far b) perhaps far off the most probable
value for a specific protein.
Best, BR
, so it's not particularly
high) I would like to add that, provided you have enough material, you can
estimate the solubility of your protein by concentrating it in a
concentrator and plotting the concentration over time without resuspending
the supernatant.
That's only a rough estimate but it's a starting point.
On Fri, Mar 05, 2010 at 03:02:55PM +0100, Jan Rash wrote:
> Dear All,
>
> This is about the crystallization of the macromolecular complex which
> is highly soluble and shows no signs of the aggregation (even at high
> concentration). We have tried several salts, precipitants and even
> high protein concentration (around 20g/L) for its crystallization
> without any genuine hit. Any suggestions for growing the crystals of
> this macromolecular complex will be highly appreciated.
>
> Thanks,
>
> Jan
--
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Tim Gruene
Institut fuer anorganische Chemie
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D-37077 Goettingen
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