This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Cryo-electron microscopy (cryo-EM) has become a powerful tool for determining the structures of proteins, viruses and molecular complexes at near-atomic resolution. However, achievable resolution is fundamentally limited by the Nyquist sampling frequency, which is determined by detector pixel size and microscope magnification.
Once this physical limit is reached, researchers typically must recollect data at higher magnification, requiring additional microscope time, increased storage capacity and often fewer particles per image. Researchers from the Exploratory Research Center on Life and Living Systems and the National Institute for Physiological Sciences have developed a computational method called Post-Acquisition Super Resolution (PASR), which enables cryo-EM data sets to surpass conventional physical Nyquist limits after data collection. PASR works by computationally subdividing detector pixels before motion correction, allowing subtle particle motion between movie frames to recover higher-frequency structural information.
The findings are published in the journal IUCrJ. The method was successfully tested on multiple data sets, including apoferritin, adeno-associated virus, jack bean urease and the giant virus Melbournevirus, using standard cryo-EM processing software such as RELION and CryoSPARC. PASR improved map quality and enabled higher-resolution reconstructions without visible artifacts.
The approach may reduce microscope use time and data storage demands while improving analysis of large, flexible or heterogeneous biological complexes. Burton Smith et al, Post-acquisition super resolution for cryo-electron microscopy, IUCrJ (2026). DOI: 10.1107/s2052252526005348 Provided by National Institutes of Natural Sciences MA in English, copy editor since 2021 with experience in higher education and health content.
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