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> at the resolution you're working at the RMSD on bond > lengths should be ca. 0.012, not 0.02 A. Interesting statement. I agree that for very well determined small molecule structures, the overall bond length variation is about 0.014 A or so. That fits quite well with what you say. It just means that the structure should be restrained to reflect reality. But: What does coordinate rmsd exactly have to do with resolution? If the 3.5 A structure has 0.012 A rmsd, does that mean that a 1.2 A structure should have 0.005? I have a feeling that would be a serious case of over-restraining. Should not all structures reflect the same 'real world' rmsd (plus minus some minor individuality) if the restraint weights are properly selected? Maybe the small molecule/shelxl fellows may chime in here: What is the expected rmsd for a high res protein structure vs. a low res? I had a feeling that super low rmsd is partly abused as a sign of crystallographic prowess, like building fantasy stuff into nonexistent density just to have no missing residues &c &c &c... Thx, br
