3 ms·
Simply because we can't know if the 10% error is because of measurement error of the method used to produce the labels. It is therefore only speculation that ~i
by rafaelero 5y ago
Simply because we can't know if the 10% error is because of measurement error of the method used to produce the labels. It is therefore only speculation that ~it is not good enough. It could very well be even better. For us to be sure, it is necessary to repeat some crystallographies and/or find a better method to produce these labels.
- COGlory 5y ago>For us to be sure, it is necessary to repeat some crystallographies and/or find a better method to produce these labels. We have this information. And we've had it for decades. There's hundreds of duplicate structures on the PDB. There are new cryo-em structures that are nearing sub angstrom. Also, the xray data we do have is never considered absolute, but the boundaries and margin of error have been quite well understood for some time.
- rafaelero 5y agoSo you are saying that it underperforms even taking into account measurement error? Can you point to an expert agreeing with your position?
- COGlory 5y agoYes, click on my bio. I'm a PhD structural biologist.
- vntok 5y agoHopefully you agree with yourself, yes, however the parent was asking for a pointer to someone else who agreed with your position.
- COGlory 5y agoOk, how about the featured article? Or the CASP competition? Or posted further up: https://www.science.org/content/blog-post/more-protein-folding-progress---what-s-it-mean https://www.science.org/content/blog-post/more-protein-foldi... Or take the RMSD of a superposition of any two identical structures on the PDB?