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4V1W

3D structure of horse spleen apoferritin determined by electron cryomicroscopy

Summary for 4V1W
Entry DOI10.2210/pdb4v1w/pdb
EMDB information2788
DescriptorFERRITIN LIGHT CHAIN (1 entity in total)
Functional Keywordsstorage protein, iron storage, iron transport, ferritins, apoferritins, horses, metals, spleen
Biological sourceEQUUS CABALLUS (HORSE)
Total number of polymer chains24
Total formula weight476938.27
Authors
Russo, C.J.,Passmore, L.A. (deposition date: 2014-10-02, release date: 2014-12-10, Last modification date: 2024-05-08)
Primary citationRusso, C.J.,Passmore, L.A.
Electron Microscopy. Ultrastable Gold Substrates for Electron Cryomicroscopy.
Science, 346:1377-, 2014
Cited by
PubMed Abstract: Despite recent advances, the structures of many proteins cannot be determined by electron cryomicroscopy because the individual proteins move during irradiation. This blurs the images so that they cannot be aligned with each other to calculate a three-dimensional density. Much of this movement stems from instabilities in the carbon substrates used to support frozen samples in the microscope. Here we demonstrate a gold specimen support that nearly eliminates substrate motion during irradiation. This increases the subnanometer image contrast such that α helices of individual proteins are resolved. With this improvement, we determine the structure of apoferritin, a smooth octahedral shell of α-helical subunits that is particularly difficult to solve by electron microscopy. This advance in substrate design will enable the solution of currently intractable protein structures.
PubMed: 25504723
DOI: 10.1126/SCIENCE.1259530
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.7 Å)
Structure validation

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