title: Reliable quality-control methods for protein crystal structures.
abstract: The emergence of structure-determination initiatives that employ high-throughput protein crystallography emphasizes the need to establish quality-control methods for screening the resulting models prior to deposition with the public data banks. An in-house database of 26 new protein structures, associated diffraction data and high-quality experimentally determined electron-density maps have been used to develop (i) a set of minimal global quality criteria that a structure must meet before the refinement may be considered completed and (ii) a reliable set of indicators for detecting local errors in protein structures. These criteria have been applied to detecting local errors to a set of structures recently deposited in the Protein Data Bank and it is estimated that about 3% of amino acids are incorrectly modeled.
authors.affiliation: Structural GenomiX, 10505 Roselle Street, San Diego, California 92121, USA. john_badger@stromix.com
authors.forename: John
authors.initials: J
authors.lastname: Badger
authors.forename: Jörg
authors.initials: J
authors.lastname: Hendle
mesh_terms: D003461:Crystallography / Q000379:methods / Q000592:standards; D030562:Databases, Protein; D004583:Electrons; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D011786:Quality Control; D015203:Reproducibility of Results; D012984:Software; D017749:Total Quality Management / Q000379:methods*
chemical_list: D011506:Proteins