Hi Tony, I always feel some people are too "greedy" with the resolution they want to > achieve. I mostly find that extremely high density is a pain to work with > as it's usually accompanied by many dual, triple conformers, a lot of noise > in the solvent phase that is often difficult to interpret, etc... Often you > spend more time on a high resolution structure that clearly shows your > protein, as opposed to a low resolution structure where it's difficult to > interpret parts of the map. Also, in most cases you REALLY don't need a 1 > Ang map to clearly show the overall structure of your protein, ligands, > first shell of solvent molecules on the surface of your protein, etc... >
higher resolution typically means you have a chance to obtain a more accurate atomic model of a crystal structure, which in turn may lead to a more accurate interpretation of this model. I fully agree that high resolution requires more modeling effort. There is still a great room for software developers to provide more automation. > Your completeness is 90% in your high resolution shell, which is fine, but > have you checked you can clearly see most reflections for h, k and l? Maybe > you're missing many reflections for one of them. I would at least > try cutting your data back to 1.1 or 1.2 Ang, as it might dramatically > improve your R factors and still show everything you want to show. > > > Also, did you try TLS refinement? > At resolutions like 1.2A or better one normally models ADPs as anisotropic for all atoms (except H), so no need to use TLS. Pavel ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1
