Have you considered it to be a disordered terminus with some waters
extending the density (at least in B1 from your figures)?
Anthony
________________________________
Anthony Addlagatta, PhD
Institute of Molecular Biology
University of Oregon
Eugene, OR-97403
Phone: (541) 346-5867
Fax: (541)346-5870
Web: http://uoregon.edu/~anthony
On Sep 28, 2007, at 1:01 PM, Jie Liu wrote:
Sure, here they are.
There are three copies in ASU, all have more or less similar
density, blue contour at 1.0sigma for 2fo-fc and magenta
at 2.5sigma for fo-fc. The shown residues are the second
valines which fit well.
Thanks.
Jie
[EMAIL PROTECTED] wrote:
Can you show the map?
Anthony
Dear all
I am refining a peptide structure with an N-terminal throenine.
However, the density map of the N-terminal part looks strange,
the first throenine does not fit in well while the second valine
fits very well. It seems that this throenine was modified somehow
during protein production. The peptide was expressed in E.Coli
and cleavaged by Formic Acid and Cyanogen Bromide, then
purified by HPLC and lyophilized.
Does anyone have similar experience of a modified N-terminal
throenine? If so, please kindly point to me a reference.
Thank you.
Jie Liu
<A1.jpg>
<B1.jpg>
<C1.jpg>
