Dear all,
I can get large amounts of a protein that is purified from inclusion
bodies. The protein is solubilized using 6M urea and refolded by dialysis.
However, treatment with urea is known to modify proteins
(N-term/Lys/Arg), which could ultimately effect crystallization.
Is this something that people generally worry about?
For example
-would you bother cleaning up the urea by ion exchange
-get ultra pure urea (ultra $$$)
-change to guanidinium chloride
-hope that it might benefit crystallization (i.e. similar to methylation
of lysines)
Thanks in advance,
Meindert
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Meindert H. Lamers
Medical Research Council
Laboratory of Molecular Biology
Hills Road,
Cambridge, CB2 0QH
United Kingdom
tel +44 (0)1223 402401
fax +44 (0)1223 213556
web: http://www2.mrc-lmb.cam.ac.uk/groups/mlamers/
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