title: Local error estimates dramatically improve the utility of homology models for solving crystal structures by molecular replacement.
abstract: Predicted structures submitted for CASP10 have been evaluated as molecular replacement models against the corresponding sets of structure factor amplitudes. It has been found that the log-likelihood gain score computed for each prediction correlates well with common structure quality indicators but is more sensitive when the accuracy of the models is high. In addition, it was observed that using coordinate error estimates submitted by predictors to weight the model can improve its utility in molecular replacement dramatically, and several groups have been identified who reliably provide accurate error estimates that could be used to extend the application of molecular replacement for low-homology cases.
authors.affiliation: Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK.
authors.forename: Gábor
authors.initials: G
authors.lastname: Bunkóczi
authors.affiliation: IFM, Linköping University, S-581 83 Linköping, Sweden.
authors.forename: Björn
authors.initials: B
authors.lastname: Wallner
authors.affiliation: Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK. Electronic address: rjr27@cam.ac.uk.
authors.forename: Randy J
authors.initials: RJ
authors.lastname: Read
mesh_terms: D018360:Crystallography, X-Ray / Q000379:methods*; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D015203:Reproducibility of Results; D012107:Research Design; D017386:Sequence Homology, Amino Acid
chemical_list: D011506:Proteins