VISUALIZATION SOFTWARE FOR ELECTRON MICROSCOPY

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 我们正在开发用于交互分析三维图像的软件 通过电子显微镜(EM)获得密度图。分析的目的是 为了确定分子机器的结构和内部工作原理，例如 作为病毒、核糖体、微管和马达、肌丝和 其他几十个系统是目前研究的目标。它是 认为活着的有机体中的大多数蛋白质都是大分子 分子组装。过去实验方法的进展 几年的时间大大加快了对这些系统的研究。这个 电磁场密度图原始数据库 (http://www.ebi.ac.uk/msd-srv/emsearch/index.html)成立于2002年 现在(2010)有773个条目。用于从以下位置推断结构的软件 许多实验室正在积极开发这些地图。 我们的软件显示密度图的等高线表面。地图来自 电子显微镜的分辨率在5-100埃范围内 它太粗糙了，看不到原子的细节。分析涉及到拟合 从结晶学到地图的已知原子结构， 在图谱中识别与未知蛋白质相对应的结构， 并比较同一系统在不同实验条件下的地图 推导配体或配体的构象变化或结合的条件 特定的大分子。我们的软件工具，是 加州大学旧金山分校嵌合体分子建模包，支架贴合，雕刻 密度区域，为地图上色，以及在地图中构建粗糙的模型。 在过去，我们已经添加了沿 显示密度值的任意定向可移动平面 剖切面。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We are developing software for interactively analyzing 3-dimensional density maps obtained by electron microscopy (EM). The analysis aims to determine structures and inner workings of molecular machines such as viruses, ribosomes, microtubules and motors, muscle filaments, and dozens of others systems that are targets of current research. It is believed that most proteins in living organisms are parts of large molecular assemblies. Advances in experimental methods in the past several years have greatly accelerated research on these systems. The primary database of EM density maps (http://www.ebi.ac.uk/msd-srv/emsearch/index.html) was founded in 2002 and now (2010) has 773 entries. Software for deducing structures from these maps is being actively developed by many labs. Our software displays contour surfaces of density maps. Maps from electron microscopy have resolutions in the 5 - 100 Angstrom range which is too coarse to see atomic detail. Analysis involves fitting known atomic structures from crystallography into the maps, identifying structures in maps corresponding to unidentified proteins, and comparing maps of the same system under different experimental conditions to deduce conformational changes or binding of ligands or specific macromolecules. Our software tools, which are part of the UCSF Chimera molecular modeling package, support fitting, carving out density regions, coloring maps, and building coarse models in maps. In the past we have added the ability to slice maps along an arbitrarily oriented and movable plane displaying density values on the cut surface.