Reverse vapour diffusion?

Steve Bryson steve at gene4d.med.utoronto.ca
Tue Mar 28 11:21:57 EST 1995


I have crystallized a protein, apparently by reverse vapour diffusion.
Due to the presence of salt, required to maintain the protein's 
solubility at high concentraions, the ionic strength of the mixed drop
is higher than the well solution when using the hanging drop technique.
Consequently, the drop grows in size and following a 5-7 day incubation
the crystals appear. When the crystals stop growing, there is little,
if any precipitate remaining.

Unfortunately there are many small crystals which appear to nucleate
on the large amounts of precipitate that is present when the crystals 
first appear.
 
I'm looking for ideas on how to improve the size of the crystals.

Steve Bryson
Dept. of Biochemistry
University of Toronto

e-mail: steve at gene4d.med.utoronto.ca

        
          
        








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