Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

By A. Brünger. 1992

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Citations in the corpus

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix (2019, methodology): “For cross-validation, Rfree is calculated on a subset of the data (typically about 2000 reflections) that are not used in refinement (Brünger, 1992).”
New tools for the analysis and validation of cryo-EM maps and atomic models (2018, methodology): “Multiple methods have been developed to identify and combat model bias (for example, Bhat & Cohen, 1984; Read, 1986; Brunger, 1992; Hodel et al., 1992).”
The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors (2014, unknown): “**Rfree is based over a subset of 5% of reflection that have not been used through the refinement [59].”
Checking your imagination: applications of the free R value. (1996, methodology): “It was suggested to use 10% of a unique set of reflections as the test data set [3].”
Conformer Generation with OMEGA: Algorithm and Validation Using High Quality Structures from the Protein Databank and Cambridge Structural Database (2010, background): “23 In this work, we demand that a structure must have a R free within 0.05 of the R -factor.”
Phi/psi-chology: Ramachandran revisited. (1996, methodology): “We have also looked at Ramachandran plots for protein models for which a free R value [3] is quoted in the PDB entry.”
Modelling dynamics in protein crystal structures by ensemble refinement (2012, unknown): “The single structure re-refinements used the same starting structure as the ensemble refinements (alternative conformations were not removed) and were re-refined using phenix.refine (version 1.7.1) ( Afonine et al., 2012 ) and Buster (version 2.10.0) ( Bricogne et al., 2009 ).”
A reference database for circular dichroism spectroscopy covering fold and secondary structure space (2006, methodology): “The structure files chosen to define the secondary structures were based on criteria of highest resolution and low R and Rfree factors (Brunger, 1992), as well as maximum correspondence to the correct protein sequence (i.e. the fewest missing residues and the same species).”
Linking crystallographic model and data quality (2012, unknown): “A. T. B. Brünger, Nature 355, 472 (1992).”