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I had a similar case with a protein which crystallised on a drop in
ionic strength. The protein was soluble in ~100 mM K Phos, and started
forming crystals when this concentration was reduced by diluting with
water (or glycerol, which had the bonus of being a cryoprotectant). The
biggest crystals (blocks with sides up to 0.3-0.4 mm ) were obtained
after setting up a hanging drop of concentrated protein over a
reservoir of water alone (no mixing!) and allowing this drop to grow
slowly by vapour diffusion. These crystals were difficult to
cryo-protect though, so a compromise including glycerol in the reservoir
and mixing with the protein drop was found. It was certainly much easier
than fiddling with dialysis buttons, though I might have been lucky.
David
Demetres D. Leonidas wrote:
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Dear fellow crystallographers,
We are lucky enough to have a protein that crystallizes in pure water
in the fridge (4 deg). However the crystals are small (0.05 x 0.01 x
0.01 mm) and only diffract to 3.2 A on a synchrotron source. We
believe that if we manage to increase their size they might diffract
better. Do you have any suggestions or even better any conditions that
they will help ?
many thanks
Demetres
