Hi Sam, Ideally, with the R factor you are at, you should be able to build these residues in, using Coot/Ono/xtalview and then refine with shelxl. If you want to go to shelxl straightaway, you might want to refine res 9-86 as one chain and res 94-last residues as another. I guess you could mutate a wate to an acetate ion. Or just read in a pdb for acetate and move it into the density where you think it should be. The tutorial for Lysozyme actually gives tells you how to do this, but it is in xtalview. You could still get some hints from it. I believe within that there are some missing residues too, deliberately removed, but kind of like your situation. Hope this helps. Arti
> Hi > I would appreciate few things for my protein structure. Data is 1.5A. > This protein is of 400 residues. 2 molecule in the asymm unit. > Missing residues are : N-terminal 8 residues, C-terminal 5 residues and in > the middle residues 87-93. > Final R(working) = 21% after refmac refinement. Some (not all) waters > created into the structure. > I am taking this structure into Shelxl for further refinement and building > the missing residues. > (1) During Shexl refinement how the missing residues I can fix. what kind > of keyword I should use to fix the missing residues with a reasonable > Occunany and B value. > (2) In COOT how can I build acetate ions in place of waters. Or any other > way I can call acetate ions. > > Thanks > Sam > > _________________________________________________________________ > Win a Zunemake MSN® your homepage for your chance to win! > http://homepage.msn.com/zune?icid=hmetagline > Arti S. Pandey Graduate Student Chemistry and Biochemistry Montana State University Bozeman,MT 59717
