Gruene Tim, Hahn Hinrich W, Luebben Anna V, Meilleur Flora, Sheldrick George M
Department of Structural Chemistry, Georg-August-University Göttingen, Tammannstrasse 4, D-37077 Göttingen, Germany.
North Carolina State University, Raleigh, NC 27695, USA ; Oak Ridge National Laboratory, Oak Ridge, TN 37831-6142, USA.
J Appl Crystallogr. 2013 Dec 7;47(Pt 1):462-466. doi: 10.1107/S1600576713027659. eCollection 2014 Feb 1.
Some of the improvements in make convenient to use for refinement of macromolecular structures against neutron data without the support of X-ray data. The new NEUT instruction adjusts the behaviour of the SFAC instruction as well as the default bond lengths of the AFIX instructions. This work presents a protocol on how to use for refinement of protein structures against neutron data. It includes restraints extending the Engh & Huber [ (1991), A, 392-400] restraints to H atoms and discusses several of the features of that make the program particularly useful for the investigation of H atoms with neutron diffraction. is already adequate for the refinement of small molecules against neutron data, but there is still room for improvement, like the introduction of chain IDs for the refinement of macromolecular structures.
中的一些改进使得在没有X射线数据支持的情况下，利用其对大分子结构进行中子数据精修变得方便。新的NEUT指令调整了SFAC指令的行为以及AFIX指令的默认键长。这项工作提出了一个关于如何利用 对蛋白质结构进行中子数据精修的方案。它包括将Engh和Huber [ (1991), A, 392 - 400]的约束扩展到H原子的约束，并讨论了 程序的几个特性，这些特性使得该程序对于用中子衍射研究H原子特别有用。 已经足以对小分子进行中子数据精修，但仍有改进的空间，比如引入链ID用于大分子结构的精修。
