Raynals, an online tool for the analysis of dynamic light scattering.

IF 2.6 4区生物学 Q2 BIOCHEMICAL RESEARCH METHODS Acta Crystallographica. Section D, Structural Biology Pub Date : 2023-08-01 DOI:10.1107/S2059798323004862

Osvaldo Burastero, George Draper-Barr, Bertrand Raynal, Maelenn Chevreuil, Patrick England, Maria Garcia Alai

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引用次数: 1

Abstract

Dynamic light scattering (DLS) is routinely employed to assess the homogeneity and size-distribution profile of samples containing microscopic particles in suspension or solubilized polymers. In this work, Raynals, user-friendly software for the analysis of single-angle DLS data that uses the Tikhonov-Phillips regularization, is introduced. Its performance is evaluated on simulated and experimental data generated by different DLS instruments for several proteins and gold nanoparticles. DLS data can easily be misinterpreted and the simulation tools available in Raynals allow the limitations of the measurement and its resolution to be understood. It was designed as a tool to address the quality control of biological samples during sample preparation and optimization and it helps in the detection of aggregates, showing the influence of large particles. Lastly, Raynals provides flexibility in the way that the data are presented, allows the export of publication-quality figures, is free for academic use and can be accessed online on the eSPC data-analysis platform at https://spc.embl-hamburg.de/.

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Raynals，动态光散射分析的在线工具。

动态光散射(DLS)通常用于评估悬浮或溶解聚合物中含有微观颗粒的样品的均匀性和尺寸分布剖面。在这项工作中，Raynals是一款用户友好的软件，用于分析使用Tikhonov-Phillips正则化的单角度DLS数据。利用不同DLS仪器对几种蛋白质和金纳米颗粒的模拟和实验数据对其性能进行了评价。DLS数据很容易被误解，Raynals提供的模拟工具允许理解测量及其分辨率的局限性。它被设计为在样品制备和优化过程中解决生物样品质量控制的工具，它有助于检测聚集体，显示大颗粒的影响。最后，Raynals在数据呈现方式上提供了灵活性，允许导出出版质量的数据，免费供学术使用，并且可以在eSPC数据分析平台https://spc.embl-hamburg.de/上在线访问。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Acta Crystallographica. Section D, Structural Biology BIOCHEMICAL RESEARCH METHODSBIOCHEMISTRY &-BIOCHEMISTRY & MOLECULAR BIOLOGY

CiteScore

4.50

自引率

13.60%

发文量

216

期刊介绍： Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them. Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged. Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.