Hi Ray,
Beyond what has already been mentioned and anecdotal evidence, at least
one structural genomics consortium
solves a substantial number, if not most, of its proteins from crystals
grown in the presence of 5-10% glycerol.
You can search crystallization conditions as well as protein
preparations for the structures (Materials and Methods) here:
http://www.thesgc.org/structures/
Just my 2-cents.
Florian
On Thu, 10 Mar 2011 17:57:02 -0500, "Edward A. Berry"
<ber...@upstate.edu> wrote:
I think adding 5% glyecrol has a big effect on the solubility, so
conditions would have to be re-optimized if glycerol is included.
In the case i am aware of also solubility was increased, but that
could be compensated by higher PEG and/or lower salt concentration
(in the salting-in region).
There are really two questions here: If crystallization conditions
have already been optimized, will adding glycerol interfere with
crystallization? probably yes. If I am starting work on crystallizing
a new protein and I know it is stabilized by glycerol, should I
avoid glycerol? No.
eab
Clayton, Gina Martyn wrote:
Hi Ray
I have seen glycerol at less than 5% in the protein buffer prevent
crystal growth completely and when removed from the buffer has
resulted
in very nice crystal growth of the glycerol free protein.
Best
Gina
------------------------------------------------------------------------
*From:* CCP4 bulletin board on behalf of Ray Brown
*Sent:* Thu 10/03/2011 17:04
*To:* CCP4BB@JISCMAIL.AC.UK
*Subject:* [ccp4bb] glycerol
Hi all,
I was intrigued by the recent question of whether glycerol had any
adverse effects on the final purity of protein isolated by
chromatography. Glycerol certainly helps to solubilize some
proteins.
Does anyone know of any negative effects of glycerol in protein
purification, on protein crystal quality or use in
cryocrystallography
and on X-ray diffraction results?
Cheers.
Ray Brown
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