31YO image
Deposition Date 2026-06-29
Release Date 2026-08-26
Last Version Date 2026-10-14
Entry Detail
PDB ID:
31YO
Keywords:
METAL BINDING PROTEIN
Title:
Horse spleen Apoferritin 0.45 MGy variable temperature dose series, 100 K
Biological Source:
Source Organism(s):
Equus caballus (Taxon ID: 9796)
Expression System(s):
Equus caballus
Method Details:
Experimental Method:
X-RAY DIFFRACTION
Resolution:
2.15 Å
R-Value Free:
0.22
R-Value Work:
0.19
R-Value Observed:
0.19
Space Group:
F 4 3 2
31YO validation report missing
Macromolecular Entities
Structures with similar UniProt ID
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:Ferritin light chain
Gene (Uniprot):FTL
Chain IDs:A (auth: X)
Chain Length:174
Number of Molecules:1
Biological Source:Equus caballus
UniProt ID:P02791 Pfam ID:PF00210
Ligand Molecules
CD
Primary Citation
Separating the effects of temperature and absorbed X-ray dose on unit-cell volume.
Acta Crystallogr D Struct Biol 82 1155 1168 (2026)
PMID: 42741972 DOI: 10.1107/S2059798326008612

Abstact

The behaviour of the unit-cell volume of crystals of the iron-storage molecule ferritin, both in the apo and the holo form, and of influenza A virus subtype N9 neuraminidase at 100 K and over a controlled cryo-temperature series was investigated. The purpose of this study was to separate out the effects of dose and temperature on the protein by assessing the changes in the unit-cell volume. Over the wide range of X-ray doses examined in this work, the irreversible effect of dose on the unit-cell volume could be distinguished from the reversible (below 160 K) temperature-induced effects. Specific structural damage effects were not reversible.

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Protein

Chemical

Disease

Primary Citation of related structures
31YO
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