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22ix

cryo-ET subtomogram-averaged structure of mouse heavy-chain apoferritin resolved at 2.71 Angstroms

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Ferritin heavy chain

Mus musculus

UniProt P09528

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 24 MAGNESIUM ION × 38 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
8j5a 8j5a

2 assemblies

Homodimer

None

Homotetramer

None

Other homooligomers
22fx 22ix 23wj 3wnw 5oba 5obb 6s61 6sht 6v21 7a4m 7kod 8bk9

25 assemblies; showing the first 12

Heteromeric or nucleic-acid complex
7tb3 7tbh

2 assemblies

View Construct and Data Evidence
UniProt name FRIH_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–182； UniProt 1–182 Author chain B； PDBConstruct 1–182； UniProt 1–182 Author chain C； PDBConstruct 1–182； UniProt 1–182 Author chain D； PDBConstruct 1–182； UniProt 1–182 Author chain E； PDBConstruct 1–182； UniProt 1–182 Author chain F； PDBConstruct 1–182； UniProt 1–182 Author chain G； PDBConstruct 1–182； UniProt 1–182 Author chain H； PDBConstruct 1–182； UniProt 1–182 Author chain I； PDBConstruct 1–182； UniProt 1–182 Author chain J； PDBConstruct 1–182； UniProt 1–182 Author chain K； PDBConstruct 1–182； UniProt 1–182 Author chain L； PDBConstruct 1–182； UniProt 1–182 Author chain M； PDBConstruct 1–182； UniProt 1–182 Author chain N； PDBConstruct 1–182； UniProt 1–182 Author chain O； PDBConstruct 1–182； UniProt 1–182 Author chain P； PDBConstruct 1–182； UniProt 1–182 Author chain Q； PDBConstruct 1–182； UniProt 1–182 Author chain R； PDBConstruct 1–182； UniProt 1–182 Author chain S； PDBConstruct 1–182； UniProt 1–182 Author chain T； PDBConstruct 1–182； UniProt 1–182 Author chain U； PDBConstruct 1–182； UniProt 1–182 Author chain V； PDBConstruct 1–182； UniProt 1–182 Author chain W； PDBConstruct 1–182； UniProt 1–182 Author chain X； PDBConstruct 1–182； UniProt 1–182

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id22ix
Deposition date deposition_date2026-01-13
Structure title titlecryo-ET subtomogram-averaged structure of mouse heavy-chain apoferritin resolved at 2.71 Angstroms
Keywords keywordscryo-ET, subtomogram-average, mouse heavy-chain apoferritin, 2.71 Angstroms, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

22ix__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

22ix__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

22ix__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）53.79 Å
Rg (electron density)52.82 Å
Total Rg53.18 Å
Atom count34238
Residues4176
Excluded volume601860 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 22ix__assembly_1__model_1 24-meric （24） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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7. Citations (1)