Protein NMR structures refined with Rosetta have higher accuracy relative to corresponding X-ray crystal structures.

ABSTRACT: We have found that refinement of protein NMR structures using Rosetta with experimental NMR restraints yields more accurate protein NMR structures than those that have been deposited in the PDB using standard refinement protocols. Using 40 pairs of NMR and X-ray crystal structures determined by the Northeast Structural Genomics Consortium, for proteins ranging in size from 5-22 kDa, restrained Rosetta refined structures fit better to the raw experimental data, are in better agreement with their X-ray counterparts, and have better phasing power compared to conventionally determined NMR structures. For 37 proteins for which NMR ensembles were available and which had similar structures in solution and in the crystal, all of the restrained Rosetta refined NMR structures were sufficiently accur

SUBMITTER: Mao B 

PROVIDER: S-EPMC4129517 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature