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TitleRadiation-dose effects in correlative X-ray/cryo-electron microscopy of frozen-hydrated biological samples.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 82, Issue Pt 3, Page 207-215, Year 2026
Publish dateMar 1, 2026
AuthorsThorsten B Blum / Vincent Olieric / Ana Diaz / Takashi Ishikawa / Volodymyr M Korkhov /
PubMed AbstractIn cryo-electron microscopy (cryo-EM), imaging of biological specimens is restricted by the limited field of view and by sample thickness. Hard X-ray imaging, with its ability to penetrate samples ...In cryo-electron microscopy (cryo-EM), imaging of biological specimens is restricted by the limited field of view and by sample thickness. Hard X-ray imaging, with its ability to penetrate samples several tens of micrometres thick, offers a complementary approach for high-resolution visualization. A major concern is whether cryo-preserved samples can withstand the handling conditions at synchrotron facilities without excessive icing, and whether the radiation exposure during X-ray imaging compromises specimen integrity, thereby hindering subsequent attempts to achieve high-resolution 3D reconstructions via cryo-EM. To evaluate this, we deposited apoferritin samples on a cryo-EM grid, exposed them to varied X-ray doses typical for X-ray tomography experiments at a synchrotron facility, and subsequently analysed the exposed particles by cryo-EM. Despite the apparent damage sustained throughout the experiment, the samples remained amenable to cryo-EM analysis, with structural details at a resolution of ∼4 Å at the highest absorbed X-ray dose of 100 MGy. By comparison, a similar cryo-EM dataset of apoferritin particles that were not exposed to X-rays but were mounted on the same cryo-EM grid resulted in a 3D reconstruction at 3.17 Å resolution. Thus, while radiation damage may limit the high-resolution information in specimens processed by cryo-X-ray tomography, the cryo-preserved biological material exposed to these high X-ray doses can still be used for subsequent cryo-EM workflows aiming to obtain structural biology insights at intermediate to high resolution. These findings lay the groundwork for an integrated imaging workflow that combines X-ray and cryo-EM techniques to enable multiscale analysis of thick vitrified biological specimens.
External linksActa Crystallogr D Struct Biol / PubMed:41746258 / PubMed Central
MethodsEM (single particle)
Resolution3.17 - 3.88 Å
Structure data

EMDB-55338: Apoferritin from equine spleen, recovered from the synchrotron with 1 MGy X-ray dose
Method: EM (single particle) / Resolution: 3.56 Å

EMDB-55343: Apoferritin from equine spleen, recovered from the synchrotron with 0 MGy X-ray dose
Method: EM (single particle) / Resolution: 3.17 Å

EMDB-55344: Apoferritin from equine spleen, recovered from the synchrotron with 100 MGy X-ray dose
Method: EM (single particle) / Resolution: 3.88 Å

Source
  • Equus caballus (horse)

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