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利用声悬浮实现非接触式通用室温大分子晶体样品呈现

Non-Contact Universal Sample Presentation for Room Temperature Macromolecular Crystallography Using Acoustic Levitation.

机构信息

School of Science and Technology, Nottingham Trent University, Nottingham, NG11 8NS, UK.

Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire, OX11 0DE, UK.

出版信息

Sci Rep. 2019 Aug 27;9(1):12431. doi: 10.1038/s41598-019-48612-4.

DOI:10.1038/s41598-019-48612-4
PMID:31455801
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6712007/
Abstract

Macromolecular Crystallography is a powerful and valuable technique to assess protein structures. Samples are commonly cryogenically cooled to minimise radiation damage effects from the X-ray beam, but low temperatures hinder normal protein functions and this procedure can introduce structural artefacts. Previous experiments utilising acoustic levitation for beamline science have focused on Langevin horns which deliver significant power to the confined droplet and are complex to set up accurately. In this work, the low power, portable TinyLev acoustic levitation system is used in combination with an approach to dispense and contain droplets, free of physical sample support to aid protein crystallography experiments. This method facilitates efficient X-ray data acquisition in ambient conditions compatible with dynamic studies. Levitated samples remain free of interference from fixed sample mounts, receive negligible heating, do not suffer significant evaporation and since the system occupies a small volume, can be readily installed at other light sources.

摘要

大分子晶体学是一种评估蛋白质结构的强大而有价值的技术。通常将样品冷却至低温以最大限度地减少 X 射线束的辐射损伤效应,但低温会阻碍蛋白质的正常功能,并且此过程会引入结构伪影。以前利用声悬浮进行光束线科学的实验主要集中在朗之万号角上,该号角将大量的能量传递到受限的液滴上,并且难以准确设置。在这项工作中,使用低功率、便携式的 TinyLev 声悬浮系统与一种分配和容纳液滴的方法结合使用,该方法不使用物理样品支架来辅助蛋白质晶体学实验。这种方法促进了在与动态研究兼容的环境条件下进行高效的 X 射线数据采集。悬浮样品不受固定样品支架的干扰,几乎不会受到加热,不会发生明显的蒸发,而且由于系统体积小,因此可以很容易地安装在其他光源上。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/ae56a6e9e005/41598_2019_48612_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/12eab4597fad/41598_2019_48612_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/1180c9e48970/41598_2019_48612_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/807e16b6fdc9/41598_2019_48612_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/9d03fbcdea27/41598_2019_48612_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/ae56a6e9e005/41598_2019_48612_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/12eab4597fad/41598_2019_48612_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/1180c9e48970/41598_2019_48612_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/807e16b6fdc9/41598_2019_48612_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/9d03fbcdea27/41598_2019_48612_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf52/6712007/ae56a6e9e005/41598_2019_48612_Fig5_HTML.jpg

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