IMPROVED METHODS FOR BUILDING PROTEIN MODELS IN ELECTRON-DENSITY MAPS AND THE LOCATION OF ERRORS IN THESE MODELS
IMPROVED METHODS FOR BUILDING PROTEIN MODELS IN ELECTRON-DENSITY MAPS AND THE LOCATION OF ERRORS IN THESE MODELS
复制标题
DOI：
10.1107/s0108767390010224
复制
发表时间：
1991-03-01
期刊：
影响因子：
--
通讯作者：
KJELDGAARD, M
中科院分区：
文献类型：
--
作者：
JONES, TA;ZOU, JY;KJELDGAARD, M
图谱解释仍然是解决大分子结构的关键步骤。 在这个早期阶段引入的错误可能在整个晶体学细化过程中持续存在，并导致不正确的结构。 通常引用的晶体学残余通常不能很好地描述模型的质量。 战略和工具描述，有助于缓解这个问题。 这些简化了模型构建过程，量化了每个残基基础上的模型拟合优度，并定位了肽和侧链构象中可能的错误。
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.