I haven't seen cauliflower but I have seen brussel sprouts. Condtions
(esp. pH) were changing over the course of crystallization, and the
stalks and sprouts were different crystal forms.
On 05/06/13 06:17, Browning Christopher wrote:
Hi Everybody,
I was wondering if anybody had a similar case to mine. The protein I'm
working on is a tough one. Its around 75 KDa in size, and it purifies
well, but soon after the full length protein starts to autolyse.
Consequently, I don't get any hits after setting up the screens.
To get around this I digest the protein with trypsin and end up with a
stable fragment of around 25KDa. When I screen this I get many hits,
but none of them look like something that can be made into single
crystals. All the hits give me large lobe-like clusters and they look
like cauliflower heads but they are optically active. I currently have
the protein in 300mM NaCl buffer. Would dropping or increasing the
salt or even using a different salt make any difference? Any ideas?
Cheers,
Chris
--
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All Things Serve the Beam
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David J. Schuller
modern man in a post-modern world
MacCHESS, Cornell University
schul...@cornell.edu
