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- EMDB-76790: Rabbit Aldolase, Laser Phase Plate TEM, Laser-ON dataset 1 (A1) -

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Basic information

Entry
Database: EMDB / ID: EMD-76790
TitleRabbit Aldolase, Laser Phase Plate TEM, Laser-ON dataset 1 (A1)
Map data
Sample
  • Organelle or cellular component: Rabbit Aldolase
Keywordscommon standard / OXYGEN TRANSPORT
Biological speciesOryctolagus cuniculus (rabbit)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.58 Å
AuthorsPetrov PN / Zhang JT / Remis JP / Axelrod JJ / Cheng H / Cooper E / Hicklin IK / Sandhaus S / Schnurr C / Glaeser RM / Mueller HM
Funding support United States, 1 items
OrganizationGrant numberCountry
Chan Zuckerberg Initiative2025-367757 United States
CitationJournal: Science / Year: 2026
Title: Laser phase plate improves structure determination of small proteins by cryo-EM.
Authors: Petar N Petrov / Jessie T Zhang / Jonathan Remis / Jeremy J Axelrod / Hang Cheng / Eric S Cooper / Ian K Hicklin / Shahar Sandhaus / Cooper Schnurr / Robert M Glaeser / Holger Müller /
Abstract: Phase plates can, in principle, overcome the poor image contrast in cryo-electron microscopy (cryo-EM) and the resulting limits on the structural reconstruction of small proteins. However, previous ...Phase plates can, in principle, overcome the poor image contrast in cryo-electron microscopy (cryo-EM) and the resulting limits on the structural reconstruction of small proteins. However, previous designs have been unstable and compromised the high-resolution signal and have thus been unable to surpass results achieved by standard cryo-EM. Here, we show that the laser phase plate (LPP), installed in a modern, custom Titan Krios microscope, enhances the resolution in single-particle reconstruction of small proteins by improving specimen-motion correction and recovery of information from the early frames, as well as particle visualization, three-dimensional classification, and alignment. These advances use standard defocus ranges and reconstruction procedures but open the door to LPP-tailored protocols, offering further improvements by leveraging the LPP demonstrated here.
History
DepositionApr 20, 2026-
Header (metadata) releaseJul 1, 2026-
Map releaseJul 1, 2026-
UpdateJul 22, 2026-
Current statusJul 22, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_76790.png

Downloads & links

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Map

FileDownload / File: emd_76790.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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Contrast
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AxesZ (Sec.)Y (Row.)X (Col.)
0.94 Å/pix.
x 200 pix.
= 188. Å		0.94 Å/pix.
x 200 pix.
= 188. Å		0.94 Å/pix.
x 200 pix.
= 188. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.94 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.01
Minimum - Maximum-0.05668922 - 0.09437244
Average (Standard dev.)0.00009334627 (±0.003495767)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 188.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_76790_half_map_1.map
Projections & Slices
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Density Histograms

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Histogram (log scale)

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Half map: #1

Fileemd_76790_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : Rabbit Aldolase

EntireName: Rabbit Aldolase
Components
  • Organelle or cellular component: Rabbit Aldolase

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Supramolecule #1: Rabbit Aldolase

SupramoleculeName: Rabbit Aldolase / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Details: Purchased from Sigma
Source (natural)Organism: Oryctolagus cuniculus (rabbit) / Tissue: muscle

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration1.6 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsPhase plate: OTHER / Spherical aberration corrector: CETCOR / Energy filter - Name: TFS Selectris X / Energy filter - Slit width: 5 eV
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 0.75 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: D2 (2x2 fold dihedral) / Resolution.type: BY AUTHOR / Resolution: 2.58 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5.0) / Number images used: 12860
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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