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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Amyloid structure determination in RELION RELION ‐3.1
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Amyloid structure determination in RELION RELION ‐3.1

机译：淀粉样蛋白结构测定RELION RELION

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摘要

Helical reconstruction in RELION is increasingly being used to determine the atomic structures of amyloid filaments from electron cryo‐microscopy (cryo‐EM) images. However, because the energy landscape of amyloid refinements is typically fraught with local optima, amyloid structure determination is often difficult. This paper aims to help RELION users in this process. It discusses aspects of helical reconstruction that are particularly relevant to amyloids, it illustrates the problem of local optima in refinement and how to detect them, and it introduces a new method to calculate 3D initial models from reference‐free 2D class averages. By providing starting models that are closer to the global optimum, this method makes amyloid structure determination easier. All methods described are open‐source and distributed within RELION ‐3.1. Their use is illustrated using a publicly available data set on tau filaments from the brain of an individual with Alzheimer's disease.
机译：螺旋重建RELION越来越多被用来确定的原子结构淀粉样纤维的低温电子显微镜低温(EM)应承担的图像。改进通常是淀粉样蛋白的景观充满了当地的最适条件,淀粉样结构决心往往是困难的。在这个过程中帮助RELION用户。讨论了螺旋重建方面特别相关的淀粉,吗说明了当地最适条件的问题精化和如何检测,它介绍了一种新方法来计算三维初始从引用量免费2 d类平均模型。提供起始模型更接近全球最优,该方法使淀粉样蛋白结构的决心更容易。描述的来源和分布在开放RELION 3.1。公开的数据集在τ细丝一个人的大脑与阿尔茨海默氏症疾病。

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