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TitleCorrection of preferred orientation-induced distortion in cryo-electron microscopy maps.
Journal, issue, pagesSci Adv, Vol. 10, Issue 30, Page eadn0092, Year 2024
Publish dateJul 26, 2024
AuthorsDongjie Zhu / Weili Cao / Junxi Li / Chunling Wu / Duanfang Cao / Xinzheng Zhang /
PubMed AbstractReconstruction maps of cryo-electron microscopy (cryo-EM) exhibit distortion when the cryo-EM dataset is incomplete, usually caused by unevenly distributed orientations. Prior efforts had been ...Reconstruction maps of cryo-electron microscopy (cryo-EM) exhibit distortion when the cryo-EM dataset is incomplete, usually caused by unevenly distributed orientations. Prior efforts had been attempted to address this preferred orientation problem using tilt-collection strategy and modifications to grids or to air-water interfaces. However, these approaches often require time-consuming experiments, and the effect was always protein dependent. Here, we developed a procedure containing removing misaligned particles and an iterative reconstruction method based on signal-to-noise ratio of Fourier component to correct this distortion by recovering missing data using a purely computational algorithm. This procedure called signal-to-noise ratio iterative reconstruction method (SIRM) was applied on incomplete datasets of various proteins to fix distortion in cryo-EM maps and to a more isotropic resolution. In addition, SIRM provides a better reference map for further reconstruction refinements, resulting in an improved alignment, which ultimately improves map quality and benefits model building.
External linksSci Adv / PubMed:39058771
MethodsEM (single particle)
Resolution3.16 - 3.8 Å
Structure data

EMDB-38080: SIRM reconstruction of the MC-45 de novo processed ribosome 50S
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-38081: Conventional Reconstruction of the MC-45 de novo processed ribosome 50S
Method: EM (single particle) / Resolution: 3.16 Å

EMDB-38082: SIRM reconstruction of the unpublished protein
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-38083: The SIRM reconstruction of the MC-40 de novo processed HA-trimer
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-38084: The conventional reconstruction of the MC-40 de novo processed HA-trimer
Method: EM (single particle) / Resolution: 3.38 Å

EMDB-38085: The SIRM reconstruction of the MC-45 de novo processed PS1
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-38086: The conventional reconstruction of the MC-45 de novo processed PS1
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-39299: Human resource SGLT1-MAP17 complex
Method: EM (single particle) / Resolution: 3.3 Å

Source
  • Escherichia coli (E. coli)
  • Homo sapiens (human)
  • Chlamydomonas reinhardtii (plant)
  • santria sp sf9 (fall armyworm)

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