α-SAS: an integrative approach for structural modeling of biological macromolecules in solution,Acta Crystallographica Section D

当前位置： X-MOL 学术 › Acta Cryst. D › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

α-SAS: an integrative approach for structural modeling of biological macromolecules in solution
Acta Crystallographica Section D ( IF 2.6 ) Pub Date : 2022-07-27 , DOI: 10.1107/s2059798322006349
Eugen Mircea Anitas ₁

Affiliation

Modern small-angle scattering (SAS) experiments with neutrons (SANS) or X-rays (SAXS) combined with contrast variation provide comprehensive information about the structure of large multicomponent macromolecules in solution and allow the size, shape and relative arrangement of each component to be mapped out. To obtain such information, it is essential to perform well designed experiments, in which all necessary steps, from assessing sample suitability to structure modeling, are properly executed. This paper describes α-SAS, an integrative approach that is useful for effectively planning a biological contrast-variation SAS experiment. The accurate generation of expected experimental intensities using α-SAS allows the substantial acceleratation of research into the structure and function of biomacromolecules by minimizing the time and costs associated with performing a SAS experiment. The method is validated using a few basic structures with known analytical expressions for scattering intensity and using experimental SAXS data from Arabidopsis β-amylase 1 protein and SANS data from the histidine kinase–Sda complex and from human dystrophin without and with a membrane-mimicking nanodisk. Simulation of a SANS contrast-variation experiment is performed for synthetic nanobodies that effectively neutralize SARS-CoV-2.

中文翻译：

α-SAS：溶液中生物大分子结构建模的综合方法

中子 (SANS) 或 X 射线 (SAXS) 结合对比度变化的现代小角散射 (SAS) 实验提供了有关溶液中多组分大分子结构的全面信息，并允许每个组分的大小、形状和相对排列被映射出来。要获得此类信息，必须进行精心设计的实验，其中从评估样品适用性到结构建模的所有必要步骤都得到正确执行。本文介绍了 α-SAS，这是一种综合方法，可用于有效规划生物对比度变化 SAS 实验。使用 α-SAS 准确生成预期的实验强度可以通过最大限度地减少与执行 SAS 实验相关的时间和成本来显着加速对生物大分子的结构和功能的研究。该方法使用一些具有已知散射强度分析表达式的基本结构和使用来自的实验 SAXS 数据进行验证来自组氨酸激酶-Sda 复合物和人肌营养不良蛋白的拟南芥β-淀粉酶 1 蛋白和 SANS 数据，没有和有模拟膜纳米盘。对有效中和 SARS-CoV-2 的合成纳米体进行了 SANS 对比变化实验的模拟。

更新日期：2022-07-27

点击分享查看原文

点击收藏

阅读更多本刊最新论文