Improved methods for building protein models in electron density maps and the location of errors in these models.
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.
Jones
T A
TA
Department of Molecular Biology, BMC, Uppsala, Sweden.
Zou
J Y
JY
Cowan
S W
SW
Kjeldgaard
M
M
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
D011506:Proteins