I echo with Nat and support depositing both structures. Despite the fact that the 38 residues are disordered, these are 2 different proteins (chemically). The disordered residues may not lead to a better model, but they do carry information. They are there and still take up physical space, thus they may change the crystal packing. Regardless of journal requirement, i think it is good practice, and nothing to lose, to deposit both.
Yu Wai Chen On 19 Jun 2012, at 18:57, "Nat Echols" <nathaniel.ech...@gmail.com> wrote: > On Tue, Jun 19, 2012 at 8:35 AM, RHYS GRINTER > <r.grinte...@research.gla.ac.uk> wrote: >> There's no significant difference between the high res and low res proteins >> in the shared region (amino acid 38+) (r.m.s.d 0.46 A), and the while there >> is broken density for the first 38aa from the full length data it's too poor >> to model into. >> >> I want to present a figure which shows the density corresponding to the >> first 38aa and where that fits with the rest if protein molecule. What I'm >> unsure of it whether I will be required by the journal to submit a model >> from the lower resolution data to the PDB in order to present this figure. >> Bearing in mind the density doesn't allow any additional residues to be >> modelled compared to the high res. structure. > > This may be true today, but there is no guarantee that it will still > be the case in five years, or ten, or however long it takes for the > software to improve. I'd argue that anything you illustrate in the > paper should end up in the PDB anyway, but if there is any chance that > someone could improve on your structure in the future and possibly > learn something new as a result, it's worth depositing for that reason > as well. Otherwise the data will probably be lost, and we'll never > know if those extra residues could have been modeled. (Although I > suspect that it would be more helpful if the images were also > available, instead of having to start from the processed data.) > > -Nat
