Ethayathulla,
 
 
from your description, it seems likely that the 
last 10 residues of the C-termus may just be disordered, esp if you observe this 
for each monomer.  if that is true, no autobuilding program will 
help you out (as far as I know), since they aren't as 
efficient building into density that is very weak or not present at 
all.  I think manually building may be your best option which doesn't 
sound too bad since it is only 10 residues/monomer.  If you aren't using 
Coot for building, i HIGHLY recommend it, since it makes these types of tasks 
very trivial.  With that, there are a few other options you might try, 
but I recommend trying to manually build as well, since these may not 
work.  
 
1- Have you tried Resolve's Prime and Switch?  
While I have only used it once, there are many examples of PnS 
significantly helping bring out some otherwise weak/missing density.  You 
may run this from a SOLVE/RESOLVE installation via command line or, [I think] 
from within the PHENIX GUI (if i recall correctly).  here is a link 
for more info...
 
 
 
 
 
2- Another option might be to either do a 
round of density modification and/or calculate a full-omit map.  
People have reported either of these can sometimes improve weak 
density.  Again, i think these are options that you can explore within 
PHENIX.  It might be worth your while to try them before and after you 
manually build the 10 extra residues/monomer....even if you only build the 
Calpha trace or polyA.  Check out the manuals for info on how to 
set some of these things up if you aren't familiar, or just post 
your questions here again, someone will surely help.  
 
3- and if you must venture away from PHENIX 
(kidding), then the folks at GlobalPhasing might recommend you give Buster-TNT a 
try.  While i have never used it, I have heard Bricogne speak wonders about 
the density maps that B-TNT produces, giving examples of much improved density 
maps, esp where weak/no density was previously observed.  Their 
people are awesome (but not as awesome as the PHENIX support, hehe) about 
helping people out with questions and with getting the software up and running 
so it can be used.  
 
Again, if it was me, I would 
first manually build in the 10 residues from the density present, even if 
just the Calpha or polyA.  Then do density modification and make maps to 
see if any additional density is present for the side-chains.  Even a sigma 
A-weighted 2fo-fc map should help you decide if the build was useful or 
not.  If there is no improvement, then it is very likely that this region 
is simply disordered and the programs probably won't help (in my little 
experience).  It is quite common for the C- and/or N-termini of proteins to 
be disordered, esp if they are recombinantly expressed and have an 
engineered 'linker' for tag removal.  If things do look better after DM, 
then you can probably build as best as you can, and allow the 
b-factors to inflate some (or however you deal with this).  
 
I hope some of this helps you out and you are able 
to build in your last 10 residues/monomer.  If any of the programs 
mentioned above works out for you, let us know, it would be good information for 
a rainy day.  Sorry I couldn't have been more help.  Best of Luck on 
your project!
 
 
 
Cheers,
Nick
 
 
 
  
  
 
 
  ----- Original Message ----- 
  
  
  Sent: Thursday, April 19, 2007 2:18 
  AM
  Subject: [phenixbb] Remodelling using 
  Phenix
  
  hi
   
  I am doing structure at 2.3A resolution. It is a dimer not NCS. I 
  have probelm in tracing last 10 amino acids in the C-terminus in both chains. 
  Both chains come close each other and winds up. So Iam finding difficulty 
  in tracing the chain. I used phenix for rebuilding with all the amino 
  acid included. But autorebuilding is not rebuilding properly, whatever input 
  is given it rebuilds on that. Actually it should be a helix and only at lower 
  cuff off we can observe density for main chain so I tried phenix rebuild to 
  improve it but it's not working. Is there any option to use phenix. 
   
  I used rebuilding with option automatic and input coordinates and 
  sequence.
   
  plz suggest do improve the phases.
   
  
-- 
A.S.Ethayathulla
Department of 
  BIophysics
All India Institute of Medical Sciences
Ansai Nagar
New 
  Delhi-110029
India 
  
  
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