Before revision:  On 24 RNA crystallographic datasets, including a 30S ribosomal subunit and an unreleased IRES domain of hepatitis C virus, the protocol corrects the majority of steric clashes and anomalous backbone and bond geometries, as assessed by MolProbity. Furthermore, the method improves the average Rfree by 0.014 , resolves functionally important discrepancies in protein-binding kink turns and group I ribozyme active sites, and refines low-resolution structures to better match higher resolution structures.
After revision:  On 24 RNA crystallographic datasets, including a 30S ribosomal subunit and an unreleased IRES domain of hepatitis C virus, the protocol corrects the majority of MolProbity-assessed errors, improves the average Rfree by 0.014 , resolves functionally important discrepancies in protein-binding kink turns and group I ribozyme active sites, and refines low-resolution structures to better match higher resolution structures.