> (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 -- -- Tim Gruene Institut fuer anorganische Chemie Tammannstr. 4 D-37077 Goettingen GPG Key ID = A46BEE1A
