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- EMDB-41923: Structure of human Apoferritin from a multi-species dataset -

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Basic information

Entry
Database: EMDB / ID: EMD-41923
TitleStructure of human Apoferritin from a multi-species dataset
Map data
Sample
  • Complex: Recombinantly expressed human apoferritin
KeywordsapoF / ferritin / octahedral / METAL BINDING PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.38 Å
AuthorsKopylov M / Bobe D / Eng ET
Funding support United States, 1 items
OrganizationGrant numberCountry
Simons FoundationSF349247 United States
CitationJournal: Acta Crystallogr F Struct Biol Commun / Year: 2024
Title: Multi-species cryoEM calibration and workflow verification standard.
Authors: Daija Bobe / Mykhailo Kopylov / Jessalyn Miller / Aaron P Owji / Edward T Eng /
Abstract: Cryogenic electron microscopy (cryoEM) is a rapidly growing structural biology modality that has been successful in revealing molecular details of biological systems. However, unlike established ...Cryogenic electron microscopy (cryoEM) is a rapidly growing structural biology modality that has been successful in revealing molecular details of biological systems. However, unlike established biophysical and analytical techniques with calibration standards, cryoEM has lacked comprehensive biological test samples. Here, a cryoEM calibration sample consisting of a mixture of compatible macromolecules is introduced that can not only be used for resolution optimization, but also provides multiple reference points for evaluating instrument performance, data quality and image-processing workflows in a single experiment. This combined test specimen provides researchers with a reference point for validating their cryoEM pipeline, benchmarking their methodologies and testing new algorithms.
History
DepositionSep 12, 2023-
Header (metadata) releaseOct 4, 2023-
Map releaseOct 4, 2023-
UpdateApr 16, 2025-
Current statusApr 16, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_41923.png

Downloads & links

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Map

FileDownload / File: emd_41923.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 360 pix.
= 394.56 Å		1.1 Å/pix.
x 360 pix.
= 394.56 Å		1.1 Å/pix.
x 360 pix.
= 394.56 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.096 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.3
Minimum - Maximum-5.552927 - 9.413945999999999
Average (Standard dev.)-0.000059537968 (±0.30980444)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 394.56 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_41923_msk_1.map
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AxesZYX

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Half map: #1

Fileemd_41923_half_map_1.map
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Half map: #2

Fileemd_41923_half_map_2.map
Projections & Slices
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Sample components

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Entire : Recombinantly expressed human apoferritin

EntireName: Recombinantly expressed human apoferritin
Components
  • Complex: Recombinantly expressed human apoferritin

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Supramolecule #1: Recombinantly expressed human apoferritin

SupramoleculeName: Recombinantly expressed human apoferritin / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 2.5 MDa

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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 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 70.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER / Details: ab-initio reconstruction
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.38 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.3.1) / Number images used: 164200
Initial angle assignmentType: RANDOM ASSIGNMENT / Software - Name: cryoSPARC (ver. 4.3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.3.1)
FSC plot (resolution estimation)

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