mdeb_2k at yahoo.com
Thu Mar 22 13:17:57 EST 2001
This question is directed to those 'gurus' who have
expertise with His-tagged proteins to help me out of
this problem. I'm new to this "affinity tagged"
I have a protein domain which is cloned and expressed
in E.coli having an N-terminal His-tag and a Thrombin
cleavage site just after that. The idea is to get rid
of the tag for crystallisation purposes by thrombin
treatment. Can you point me to any reference(s), ideal
for a novice, having details for the same and
subsequent purification steps to eliminate the
contaminants! Any nice protocol would as well be good!
Any help would be highly appreciated.
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