| Literature DB >> 27710115 |
Jin Seob Kim1, Bijan Afsari2, Gregory S Chirikjian1.
Abstract
Cryo-electron microscopy (EM) and small angle X-ray scattering (SAXS) are two different data acquisition modalities often used to glean information about the structure of large biomolecular complexes in their native states. A SAXS experiment is generally considered fast and easy but unveils the structure at very low resolution, whereas a cryo-EM experiment needs more extensive preparation and postacquisition computation to yield a three-dimensional (3D) density map at higher resolution. In certain applications, we may need to verify whether the data acquired in the SAXS and cryo-EM experiments correspond to the same structure (e.g., before reconstructing the 3D density map in EM). In this article, a simple and fast method is proposed to verify the compatibility of the SAXS and EM experimental data. The method is based on averaging the two-dimensional correlation of EM images and the Abel transform of the SAXS data. Orientational preferences are known to exist in cryo-EM experiments, and we also consider these effects on our method. The results are verified on simulations of conformational states of large biomolecular complexes.Keywords: Abel transform; SAXS; compatibility; correlation function; cryo-EM; preferred orientations
Mesh:
Substances:
Year: 2016 PMID: 27710115 PMCID: PMC5220572 DOI: 10.1089/cmb.2016.0139
Source DB: PubMed Journal: J Comput Biol ISSN: 1066-5277 Impact factor: 1.479