Using a conformation-dependent stereochemical library improves crystallographic refinement of proteins.
The major macromolecular crystallographic refinement packages restrain models to ideal geometry targets defined as single values that are independent of molecular conformation. However, ultrahigh-resolution X-ray models of proteins are not consistent with this concept of ideality and have been used to develop a library of ideal main-chain bond lengths and angles that are parameterized by the phi/psi angle of the residue [Berkholz et al. (2009), Structure, 17, 1316-1325]. Here, it is first shown that the new conformation-dependent library does not suffer from poor agreement with ultrahigh-resolution structures, whereas current libraries have this problem. Using the TNT refinement package, it is then shown that protein structure refinement using this conformation-dependent library results in models that have much better agreement with library values of bond angles with little change in the R values. These tests support the value of revising refinement software to account for this new paradigm.
Tronrud
Dale E
DE
Department of Biophysics and Biochemistry, Oregon State University, Corvallis, Oregon 97331, USA.
Berkholz
Donald S
DS
Karplus
P Andrew
PA
D018360:Crystallography, X-Ray / Q000379:methods*; D030562:Databases, Protein; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis* / Q000737:chemistry
D011506:Proteins