National Centre for Biological Sciences, Tata Institute of Fundamental Research, GKVK Post, Bellary Road, Bengaluru 560 065, India.
Acta Crystallogr D Struct Biol. 2024 Jul 1;80(Pt 7):535-550. doi: 10.1107/S2059798324005229. Epub 2024 Jun 27.
The formation of a vitrified thin film embedded with randomly oriented macromolecules is an essential prerequisite for cryogenic sample electron microscopy. Most commonly, this is achieved using the plunge-freeze method first described nearly 40 years ago. Although this is a robust method, the behaviour of different macromolecules shows great variation upon freezing and often needs to be optimized to obtain an isotropic, high-resolution reconstruction. For a macromolecule in such a film, the probability of encountering the air-water interface in the time between blotting and freezing and adopting preferred orientations is very high. 3D reconstruction using preferentially oriented particles often leads to anisotropic and uninterpretable maps. Currently, there are no general solutions to this prevalent issue, but several approaches largely focusing on sample preparation with the use of additives and novel grid modifications have been attempted. In this study, the effect of physical and chemical factors on the orientations of macromolecules was investigated through an analysis of selected well studied macromolecules, and important parameters that determine the behaviour of proteins on cryo-EM grids were revealed. These insights highlight the nature of the interactions that cause preferred orientations and can be utilized to systematically address orientation bias for any given macromolecule and to provide a framework to design small-molecule additives to enhance sample stability and behaviour.
形成嵌入随机取向大分子的玻璃态薄膜是低温样品电子显微镜的基本前提。最常用的方法是近 40 年前首次描述的非浸润式冷冻方法。尽管这是一种稳健的方法,但不同大分子的行为在冷冻时表现出很大的差异,通常需要进行优化以获得各向同性的高分辨率重构。对于这样的薄膜中的大分子,在擦拭和冷冻之间的时间内遇到气-水界面并采用优先取向的概率非常高。使用优先取向的粒子进行 3D 重构通常会导致各向异性和不可解释的图谱。目前,对于这个普遍存在的问题没有通用的解决方案,但已经尝试了几种主要关注于使用添加剂和新型网格修改进行样品制备的方法。在这项研究中,通过分析选定的研究充分的大分子,研究了物理和化学因素对大分子取向的影响,并揭示了决定蛋白质在 cryo-EM 网格上行为的重要参数。这些见解突出了导致优先取向的相互作用的本质,可以用于系统地解决任何给定大分子的取向偏差,并提供一个设计小分子添加剂的框架,以增强样品稳定性和行为。