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 <[log in to unmask]
> <mailto:[log in to unmask]>> 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 <[log in to unmask] <mailto:[log in to unmask]>>:
> > 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 [log in to unmask] <mailto:[log in to unmask]>
> [log in to unmask] <mailto:[log in to unmask]>
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