Hi Jan,
We have tried crystallizing a similar protein without success, later on
it turned out that the protein was having a strong interaction with DNA
that was not sequence specific. You might have a case like that....
Flip
Jan Rash wrote:
Dear All,
I have a question regarding the crystallization of lysine and arginine
rich protein around 13%. So far our attempts to crystallize this protein
have not been successful although the secondary structure predictions,
CD spectroscopy measurements clearly show that this protein is folded. I
presume that these lysine and arginine are the sources of the local
flexibility in the protein even though the protein is globular overall.
Moreover, my attempts to crystallize the limited proteolysis fragments
also did not achieve crystals. I have also tried the crystallization
with its binding partners and could not succeed. I think any compound
that binds to the lysine/arginine side chains might affect the
crystallization process thereby reducing the internal flexibility of
protein. Can anybody suggest some effective strategy for the
crystallization?
Thanks
Umar
