Validation of electron-microscopy maps using solution small-angle X-ray scattering

被引:1
|
作者
Lytje, Kristian [1 ,2 ]
Pedersen, Jan Skov [1 ,2 ]
机构
[1] Aarhus Univ, Dept Chem, Gustav Wieds Vej 14, DK-8000 Aarhus, Denmark
[2] Aarhus Univ, Interdisciplinary Nanosci Ctr iNANO, Gustav Wieds Vej 14, DK-8000 Aarhus, Denmark
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2024年 / 80卷
关键词
electron microscopy; small-angle X-ray scattering; electron-microscopy validation; structure determination; PROTEIN; COMPUTATION; SAXS;
D O I
10.1107/S2059798324005497
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The determination of the atomic resolution structure of biomacromolecules is essential for understanding details of their function. Traditionally, such a structure determination has been performed with crystallographic or nuclear resonance methods, but during the last decade, cryogenic transmission electron microscopy (cryo-TEM) has become an equally important tool. As the blotting and flash-freezing of the samples can induce conformational changes, external validation tools are required to ensure that the vitrified samples are representative of the solution. Although many validation tools have already been developed, most of them rely on fully resolved atomic models, which prevents early screening of the cryo-TEM maps. Here, a novel and automated method for performing such a validation utilizing small-angle X-ray scattering measurements, publicly available through the new software package AUSAXS, is introduced and implemented. The method has been tested on both simulated and experimental data, where it was shown to work remarkably well as a validation tool. The method provides a dummy atomic model derived from the EM map which best represents the solution structure.
引用
收藏
页码:493 / 505
页数:13
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