Hard to say without seeing the maps and experimenting. My first check would be to set the NTD occupancies to 0.0 - refine the CTD alone, then look at the maps in COOT.
Or maybe let an automatic modelling building program such as Buccaneer try to rebuild the NTD section, with starting phases from the CTD. Eleanor On 13 May 2013 09:04, atul kumar <[email protected]> wrote: > Dear all, > > I have solved the structure of my protein by molecular replacement at > 2.9A, with Rfactor and Rfree 18 and 22 respectively. Overall everything > seems fine, its a two domain protein NTD and CTD, the NTD have high average > B factor compared to CTD. A helix of NTD seems to be disordered, I tried > different geometric weights but the refined structure does not seem to > follow proper geometry for this helix. The B-factor of this helix is very > high compared to overall B factor for NTD and omit map shows only some > partial density in this region( off course not conclusive). All the > homologous structure have helix in this region although with high B-factor. > Should I submit the current pdb or need more refinement? > > thanks and regards > > Atul Kumar >
