title: Improved methods for building protein models in electron density maps and the location of errors in these models.
abstract: Map interpretation remains a critical step in solving the structure of a macromolecule. Errors introduced at this early stage may persist throughout crystallographic refinement and result in an incorrect structure. The normally quoted crystallographic residual is often a poor description for the quality of the model. Strategies and tools are described that help to alleviate this problem. These simplify the model-building process, quantify the goodness of fit of the model on a per-residue basis and locate possible errors in peptide and side-chain conformations.
authors.affiliation: Department of Molecular Biology, BMC, Uppsala, Sweden.
authors.forename: T A
authors.initials: TA
authors.lastname: Jones
authors.forename: J Y
authors.initials: JY
authors.lastname: Zou
authors.forename: S W
authors.initials: SW
authors.lastname: Cowan
authors.forename: M
authors.initials: M
authors.lastname: Kjeldgaard
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003196:Computer Graphics; D003460:Crystallization; D008958:Models, Molecular; D015394:Molecular Structure; D011506:Proteins / Q000737:chemistry*; D012984:Software; D014961:X-Ray Diffraction
chemical_list: D011506:Proteins