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Hi Schreuder, Thank you for your suggestion. As per the electron density, the conformation is very obvious. So I think whatever NCS outliers are there in structure, are real ones. Thanking you all, On 24-Apr-2017 1:29 PM, <[log in to unmask]> wrote: > Dear Vipul, > > > > At this resolution and with these Rfactors you are not supposed to > „correct“ the NCS outliers. Look into the electron density maps if they are > well defined and if the different conformations can be explained by e.g. > crystal contacts. > > > > However, if they are in a less well-defined region, you should superimpose > the NCS symmetry molecule(s) and see which conformation would fit best and > fit this conformation in the other molecules as well. > > > > Best, > > Herman > > > > *Von:* CCP4 bulletin board [mailto:[log in to unmask]] *Im Auftrag von > *Vipul Panchal > *Gesendet:* Montag, 24. April 2017 09:49 > *An:* [log in to unmask] > *Betreff:* [ccp4bb] NCS difference > > > > Hi all, > > > > I am solving structure of one of the acyltransferse protein. We have > collected data at 2.16A resolution. Currently the Rfree is 0.2508 and > Rwork is 0.2042. > > > > *My query is regarding NCS difference.* Under validation tool of coot > while looking for NCS differene, i can find some residues with red bar. *Can > some one suggest me how may i minimize it if i am expected to do it?* > > > > > -- > > Vipul Panchal > > Senior Research Fellow, > > Respiratory disease and biology, > > CSIR-IGIB > > (M)-9540113372 >