Hi Sang Hoon,
You should do the refinement in BUSTER, which uses a novel method to
impose NCS restraints. These restraints (called LSSR restraints) were
designed specifically to provide an answer to your question in a
systematic way, by comparing the local environments of corresponding
residues in each copy of your protein.
Good luck,
Joe
Jim Fairman a écrit :
Sang Hoon,
Each molecule in the asymmetric unit is most likely different. I work
on a protein that crystallizes as a homodimer with 2 molecules per
asymmetric unit and there are some differences between the two (eg:
electron density visible for the 14 N-terminal residues in one
molecule, but not the other).
Cheers, Jim
On Tue, Mar 24, 2009 at 11:03 AM, Folmer Fredslund <folm...@gmail.com
<mailto:folm...@gmail.com>> wrote:
Dear Sang
They are really different!
And I guess you would probably want to use NCS restraints depending on
your resolution.
Regards,
Folmer
2009/3/24 Sang Hoon Joo <s...@duke.edu <mailto:s...@duke.edu>>:
> I am refining my crystal structure in which I have two identical
> chains in one asymmetric unit.
> Space group is H32 and each chain yields me a biological trimer
as expected.
> The problem is, do I have to assume they are identical, or they are
> really different.
> After each cycle of refinement, if I try to align two molecules
I get
> ~ 0.17 RMSD.
> --
> Sang Hoon Joo, PhD
> Postdoctoral Associate
> Duke University
> 239 Nanaline H. Duke
> Box 3711, DUMC
> Durham, NC 27710
>
--
Jim Fairman
Graduate Research Assistant
Department of Biochemistry, Cellular, and Molecular Biology (BCMB)
University of Tennessee -- Knoxville
216-368-3337 jfair...@utk.edu <mailto:jfair...@utk.edu>
james.fair...@case.edu <mailto:james.fair...@case.edu>
