2026-03-18 REL PDBe INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY INITIAL_RELEASE REPOSITORY DATABASE_REFERENCES citation citation_author em_admin _citation.journal_volume _citation.page_first _citation.page_last _citation.pdbx_database_id_PubMed _citation.title _citation_author.identifier_ORCID _citation_author.name _em_admin.last_update EXPERIMENTAL_SUMMARY citation citation_author em_admin _citation.journal_volume _citation.page_first _citation.page_last _citation.pdbx_database_id_PubMed _citation.title _citation_author.identifier_ORCID _citation_author.name _em_admin.last_update PDBe PDBe 2025-09-01 2026-02-25 2026-02-25 2026-03-18 European Union (EU) 101086665 European Union German Federal Ministry for Education and Research 03Z22HN23 Germany German Federal Ministry for Education and Research 03Z22HI2 Germany German Federal Ministry for Education and Research 03COV04 Germany European Regional Development Fund ZS/2016/04/78115 European Union European Regional Development Fund ZS/2024/05/187255 European Union German Research Foundation (DFG) 391498659 Germany German Research Foundation (DFG) 514901783 Germany Fundacao para a Ciencia e a Tecnologia UIDB/04612/2020 Portugal Fundacao para a Ciencia e a Tecnologia UIDP/04612/2020 Portugal Fundacao para a Ciencia e a Tecnologia LA/P/0087/2020 Portugal H2020 Marie Curie Actions of the European Commission 101207412 European Union Cryo-EM structure of Human Apoferritin at pH 5 Skalidis I Semchonok DA Tueting C Hamdi F Kastritis PL Apoferritin, Ferritin, Metal storage, Low pH, METAL BINDING PROTEIN Hamdi F Skalidis I Schwerin IK Belapure J Semchonok DA Kyrilis FL Tuting C Muller J Kunze G Kastritis PL Direct evidence of acid-driven protein desolvation. Proc.Natl.Acad.Sci.USA US 123 e2525949123 e2525949123 2026 41785322 doi:10.1073/pnas.2525949123 1091-6490 0040 PNASA6 9sjt FULLOVERLAP EMDB EMD-54953 associated EM volume
Cryo-EM structure of Human Apoferritin at pH 5
 24-mer of Human Apoferritin at pH 5 24-mer of Human Apoferritin at pH 5 0 1 Homo sapiens 0.5 Ferritin heavy chain, N-terminally processed Homo sapiens 0.020176599999999996 24 Escherichia coli 'BL21-Gold(DE3)pLysS AG' LEVO STSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQ DIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLSEQVKAIKELGDHVTNLRKMGAPES GLAEYLFDKHTLG P02794 FE (III) ION 5.5845e-05 24 FE MAGNESIUM ION 2.4305e-05 24 MG water 1.8015e-05 1248 HOH singleParticle particle 0.2 5.0 Quantifoil R2/1 COPPER 300 CARBON HOLEY GLOW DISCHARGE ETHANE 100 277 FEI VITROBOT MARK IV TFS GLACIOS SPOT SCAN BRIGHT FIELD FIELD EMISSION GUN 200 2.7 1.0 2.0 NITROGEN FEI FALCON III (4k x 4k) COUNTING 2541 30.0 1 521922 Gctf PHASE FLIPPING AND AMPLITUDE CORRECTION
Ab-initio model
 O SIMULTANEOUS ITERATIVE (SIRT) 1.96 FSC 0.143 CUT-OFF RELION 4 421029 MAXIMUM LIKELIHOOD RELION 4 MAXIMUM LIKELIHOOD RELION 300 cryoSPARC 3.2 emd_54953.map.gz 1 IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) 320 320 320 0 0 0 320 320 320 189.44 189.44 189.44 90.0 90.0 90.0 X Y Z -2.7933054 5.63101 0.005105555 0.31772348 0.592 0.592 0.592 0.6 AUTHOR ApoF resolved at pH 5, Map sharp Other experimental model
UniProt ID: P02794
 FLEXIBLE FIT REAL emd_54953_msk_1.map emd_54953_half_map_2.map.gz 1 IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) 320 320 320 0 0 0 320 320 320 189.44 189.44 189.44 90.0 90.0 90.0 X Y Z -0.32001284 1.0461329 0.0014261513 0.086081974 0.592 0.592 0.592 AUTHOR ApoF resolved at pH 5, Half-map A emd_54953_half_map_1.map.gz 1 IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) 320 320 320 0 0 0 320 320 320 189.44 189.44 189.44 90.0 90.0 90.0 X Y Z -0.33524847 1.0612344 0.0014485461 0.08629201 0.592 0.592 0.592 AUTHOR ApoF resolved at pH 5, Half-map B