ARP/wARP and molecular replacement
ARP/wARP and molecular replacement
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DOI：
10.1107/s0907444901014007
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发表时间：
2001-10-01
期刊：
影响因子：
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通讯作者：
Lamzin, VS
中科院分区：
文献类型：
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作者：
Perrakis, A;Harkiolaki, M;Lamzin, VS
ARP/wARP的目的是提高大分子晶体学模型建立和精化的自动化程度。一旦获得了分子替代解决方案，改进和重建初始（搜索）模型通常是乏味的。ARP/wARP提供了三种不同程度的自动化任务选项：(i)基于从分子替代方案计算的相位自动构建一个全新的模型；（ii）通过添加和删除原子来更新初始模型，以获得改进的地图；（iii）将结构对接到一个新的（或突变的）序列上，然后在真实空间中重建和精炼侧链。提出了几个例子，其中ARP/wARP在结构解决的速度方面产生了相当大的差异和/或使其他困难或无法解释的地图得以改进。目前允许完全自动构建蛋白质结构的分辨率范围为2.0埃，但对于地图改进来说，即使在3.2埃的间距上，也比更传统的精细技术有了明显的进步。
The aim of ARP/wARP is improved automation of model building and refinement in macromolecular crystallography. Once a molecular-replacement solution has been obtained, it is often tedious to refine and rebuild the initial (search) model. ARP/wARP offers three options to automate that task to varying extents: (i) autobuilding of a completely new model based on phases calculated from the molecular-replacement solution, (ii) updating of the initial model by atom addition and deletion to obtain an improved map and (iii) docking of a structure onto a new (or mutated) sequence, followed by rebuilding and refining the side chains in real space. A few examples are presented where ARP/wARP made a considerable difference in the speed of structure solution and/or made possible refinement of otherwise difficult or uninterpretable maps. The resolution range allowing complete autobuilding of protein structures is currently 2.0 Angstrom, but for map improvement considerable advances over more conventional refinement techniques are evident even at 3.2 Angstrom spacing.