32EA
Horse spleen Holoferritin 14.5 MGy variable temperature dose series, 130 K
Summary for 32EA
| Entry DOI | 10.2210/pdb32ea/pdb |
| Related | 32CO |
| Descriptor | Ferritin light chain, CADMIUM ION (3 entities in total) |
| Functional Keywords | metal storage, variable temperature dose series, metal binding protein |
| Biological source | Equus caballus (horse) |
| Total number of polymer chains | 1 |
| Total formula weight | 20097.25 |
| Authors | Southworth-Davies, R.J.,Murray, J.W.,Carmichael, I.,Rudino-Pinera, E.,Weik, M.,Garman, E.F. (deposition date: 2026-07-07, release date: 2026-08-26, Last modification date: 2026-09-30) |
| Primary citation | Southworth-Davies, R.J.,Murray, J.W.,Carmichael, I.,Rudino-Pinera, E.,Weik, M.,Garman, E.F. Separating the effects of temperature and absorbed X-ray dose on unit-cell volume. Acta Crystallogr D Struct Biol, 2026 Cited by PubMed Abstract: 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. PubMed: 42741972DOI: 10.1107/S2059798326008612 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
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