[buster-discuss] Refinement of a disordered part of a peptide

Miguel Ortiz Lombardía miguel.ortiz-lombardia at igs.cnrs-mrs.fr
Wed May 4 16:02:47 CEST 2016


I'm refining a structure at ~1.8 A including several copies of a protein
molecule in the AU. For a couple of these the N-terminus is well-behaved
and can be modelled easily. In the other copies there is some residual,
not fully-connected density suggesting that the N-termini are mostly in
the same conformation. But mostly is not the same than completely and
trying to model them in the density is not satisfactory: it seems clear
that they are moving a lot around that conformation. I have tried to
refine them with lower occupancy after fitting in the residual density,
but that's not satisfactory either. Leaving out these N-termini gives a
more correct model in terms of stereochemistry but somehow surrenders
model completeness and leaves behind those blobs.

I'd appreciate any ideas that could improve the model in a reasonable,
not over-fitted way using autoBUSTER.

Thank you!


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