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TitleUltra-rapid cryo-EM data acquisition method enabled by continuous recording based beam image shift.
Journal, issue, pagesNat Commun, Year 2026
Publish dateJun 12, 2026
AuthorsQi Yang / Xiaojun Huang / Chunling Wu / Yan Zeng / Xinzheng Zhang /
PubMed AbstractCryo-electron microscopy (cryo-EM) data acquisition is time-intensive given that a large amount of data is required to obtain a high-resolution reconstruction. Here, we eliminate camera-induced delay ...Cryo-electron microscopy (cryo-EM) data acquisition is time-intensive given that a large amount of data is required to obtain a high-resolution reconstruction. Here, we eliminate camera-induced delay time by continuously recording during beam-image shift acquisition using a method called Continuous Recording Beam-Image Shift (CR-BIS). The utilization of CR-BIS with K3 and Falcon 4 direct electron detectors and conventional data acquisition conditions enables the acquisition of ~34,000 micrographs and ~1,000 tilt series per 24 h in single-particle analysis mode and cryo-electron tomography mode, respectively. Three-dimensional reconstructions of single-particle and tomographic datasets show that CR-BIS accelerates data collection and maintains data quality. CR-BIS is broadly applicable for efficient high-resolution cryo-EM since it can be implemented into existing acquisition software through scripting and it does not require hardware modification.
External linksNat Commun / PubMed:42285946
MethodsEM (subtomogram averaging) / EM (single particle)
Resolution1.64 - 3.57 Å
Structure data

EMDB-65963: In situ subtomogram average of 80S ribosome (local refined with LSU mask)
Method: EM (subtomogram averaging) / Resolution: 3.57 Å

EMDB-68807: Cryo-EM structure of human apoferritin at 1.81 Angstrom resolution(using CR-BIS data collection on Falcon4).
Method: EM (single particle) / Resolution: 1.81 Å

EMDB-68808: Cryo-EM structure of human apoferritin at 1.79 Angstrom resolution(using BIS data collection on Falcon4).
Method: EM (single particle) / Resolution: 1.79 Å

EMDB-68809: Cryo-EM structure of human apoferritin at 1.64 Angstrom resolution(using CR-BIS data collection on Falcon4i).
Method: EM (single particle) / Resolution: 1.64 Å

EMDB-68810: Cryo-EM structure of human apoferritin at 1.65 Angstrom resolution(using BIS data collection on Falcon4i).
Method: EM (single particle) / Resolution: 1.65 Å

EMDB-68811: Cryo-EM structure of human apoferritin at 2.05 Angstrom resolution(using CR-BIS data collection on K3).
Method: EM (single particle) / Resolution: 2.05 Å

EMDB-68812: Cryo-EM structure of human apoferritin at 2.05 Angstrom resolution(using BIS data collection on K3).
Method: EM (single particle) / Resolution: 2.05 Å

EMDB-68813: Subtomogram average structure of human apoferritin at 2.21 Angstrom resolution(using CR-BIS data collection on K3).
Method: EM (subtomogram averaging) / Resolution: 2.21 Å

EMDB-68814: Subtomogram average structure of human apoferritin at 2.28 Angstrom resolution(using BIS data collection on K3).
Method: EM (subtomogram averaging) / Resolution: 2.28 Å

EMDB-68815: Subtomogram average structure of human apoferritin at 1.98 Angstrom resolution(using CR-BIS data collection on Falcon4i).
Method: EM (subtomogram averaging) / Resolution: 1.98 Å

EMDB-68816: Subtomogram average structure of human apoferritin at 2.01 Angstrom resolution(using BIS data collection on Falcon4i).
Method: EM (subtomogram averaging) / Resolution: 2.01 Å

EMDB-68817: Subtomogram average structure of human apoferritin at 2.24 Angstrom resolution(using CR-BIS data collection on Falcon4).
Method: EM (subtomogram averaging) / Resolution: 2.24 Å

EMDB-68818: Subtomogram average structure of human apoferritin at 2.34 Angstrom resolution(using BIS data collection on Falcon4).
Method: EM (subtomogram averaging) / Resolution: 2.34 Å

Source
  • Saccharomyces cerevisiae S288C (yeast)
  • Homo sapiens (human)

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