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- EMDB-65584: Cryo-EM structure of complex III on the bovine heart submitochond... -

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Basic information

Entry
Database: EMDB / ID: EMD-65584
TitleCryo-EM structure of complex III on the bovine heart submitochondrial particles, III-2
Map data
Sample
  • Complex: Complex III on the bovine heart submitochondrial particles
    • Protein or peptide: x 11 types
  • Ligand: x 3 types
Keywordsrespiratory chain complex / supercomplex / submitochondrial particles / MOTOR PROTEIN / OXIDOREDUCTASE
Function / homology
Function and homology information


Complex III assembly / subthalamus development / pons development / cerebellar Purkinje cell layer development / pyramidal neuron development / Respiratory electron transport / thalamus development / Mitochondrial translation termination / respiratory chain complex III / quinol-cytochrome-c reductase ...Complex III assembly / subthalamus development / pons development / cerebellar Purkinje cell layer development / pyramidal neuron development / Respiratory electron transport / thalamus development / Mitochondrial translation termination / respiratory chain complex III / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / Mitochondrial protein degradation / hypothalamus development / midbrain development / ubiquinone binding / respiratory electron transport chain / hippocampus development / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / mitochondrial membrane / oxidoreductase activity / mitochondrial inner membrane / heme binding / protein-containing complex / mitochondrion / proteolysis / membrane / metal ion binding
Similarity search - Function
Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Globular protein, non-globular alpha/beta subunit / Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily ...Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Globular protein, non-globular alpha/beta subunit / Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 9 superfamily / Cytochrome b-c1 complex subunit 9 / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome c1, transmembrane anchor, C-terminal / : / Cytochrome b / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / : / Cytochrome c1 / Cytochrome C1 family / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / : / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily
Similarity search - Domain/homology
Cytochrome c1, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 9 / Cytochrome b / Cytochrome b-c1 complex subunit 10 / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.4 Å
AuthorsNakano A / Masuya T / Akisada S / Ishikawa-Fukuda M / Mitsuoka K / Miyoshi H / Murai M / Yokoyama K
Funding support Japan, 3 items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)23H02453 Japan
Japan Society for the Promotion of Science (JSPS)25K01958 Japan
Ministry of Education, Culture, Sports, Science and Technology (Japan) Japan
CitationJournal: Nat Commun / Year: 2026
Title: Structures of respiratory supercomplexes and ATP synthase oligomers in mammalian mitochondrial inner membrane.
Authors: Atsuki Nakano / Takahiro Masuya / Shinsuke Akisada / Moe Ishikawa-Fukuda / Kaoru Mitsuoka / Hideto Miyoshi / Masatoshi Murai / Ken Yokoyama /
Abstract: Understanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the ...Understanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the structures of FF ATP synthase and respiratory supercomplexes (SCs) on sub-mitochondrial particles (SMPs) isolated from bovine heart mitochondria. Most FF complexes were observed as dimers stabilized by the regulatory factor IF₁, and a tetrameric assembly comprising two FF-IF₁ dimers arranged linearly was also identified. This finding indicates that the tetrameric units of FF are present in the mitochondrial inner membrane and contribute to shaping cristae tips in mammalian mitochondria. F domain maps resolve the e-subunit- c₈-ring interface and show no discrete density for a tightly bound lipid within the c₈-ring. In addition to the previously reported SCs compositions CI₁CIII₂CIV₁ and CI₁CIII₂CIV₂, our analysis identified an additional assembly with the composition CI₁CIII₂CIV₃, as well as a CI₂CIII₂CIV₆ mega-complex. This approach enables rapid structural determination of FF ATP synthase and SCs from minimal membrane fractions, providing a foundation for elucidating the molecular basis of metabolic disorders and mitochondrial diseases at the level of higher-order architecture.
History
DepositionJul 28, 2025-
Header (metadata) releaseApr 1, 2026-
Map releaseApr 1, 2026-
UpdateApr 1, 2026-
Current statusApr 1, 2026Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_65584.png

Downloads & links

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Map

FileDownload / File: emd_65584.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 600 pix.
= 654. Å		1.09 Å/pix.
x 600 pix.
= 654. Å		1.09 Å/pix.
x 600 pix.
= 654. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.09 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.3
Minimum - Maximum-0.7215469 - 1.6681243
Average (Standard dev.)-0.00040807325 (±0.031061167)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions600600600
Spacing600600600
CellA=B=C: 654.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_65584_msk_1.map
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Additional map: #1

Fileemd_65584_additional_1.map
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Half map: #1

Fileemd_65584_half_map_1.map
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Half map: #2

Fileemd_65584_half_map_2.map
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Sample components

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Entire : Complex III on the bovine heart submitochondrial particles

EntireName: Complex III on the bovine heart submitochondrial particles
Components
  • Complex: Complex III on the bovine heart submitochondrial particles
    • Protein or peptide: Cytochrome b-c1 complex subunit 1, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 2, mitochondrial
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome c1, heme protein, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 7
    • Protein or peptide: Cytochrome b-c1 complex subunit 8
    • Protein or peptide: Cytochrome b-c1 complex subunit 6, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 9
    • Protein or peptide: Cytochrome b-c1 complex subunit 9
    • Protein or peptide: Cytochrome b-c1 complex subunit 10
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: HEME C
  • Ligand: FE2/S2 (INORGANIC) CLUSTER

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Supramolecule #1: Complex III on the bovine heart submitochondrial particles

SupramoleculeName: Complex III on the bovine heart submitochondrial particles
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#11
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 500 KDa

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Macromolecule #1: Cytochrome b-c1 complex subunit 1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 1, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 49.266254 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString: TATYAQALQS VPETQVSQLD NGLRVASEQS SQPTCTVGVW IDAGSRYESE KNNGAGYFVE HLAFKGTKNR PGNALEKEVE SMGAHLNAY STREHTAYYI KALSKDLPKA VELLADIVQN CSLEDSQIEK ERDVILQELQ ENDTSMRDVV FNYLHATAFQ G TPLAQSVE ...String:
TATYAQALQS VPETQVSQLD NGLRVASEQS SQPTCTVGVW IDAGSRYESE KNNGAGYFVE HLAFKGTKNR PGNALEKEVE SMGAHLNAY STREHTAYYI KALSKDLPKA VELLADIVQN CSLEDSQIEK ERDVILQELQ ENDTSMRDVV FNYLHATAFQ G TPLAQSVE GPSENVRKLS RADLTEYLSR HYKAPRMVLA AAGGLEHRQL LDLAQKHFSG LSGTYDEDAV PTLSPCRFTG SQ ICHREDG LPLAHVAIAV EGPGWAHPDN VALQVANAII GHYDCTYGGG AHLSSPLASI AATNKLCQSF QTFNICYADT GLL GAHFVC DHMSIDDMMF VLQGQWMRLC TSATESEVLR GKNLLRNALV SHLDGTTPVC EDIGRSLLTY GRRIPLAEWE SRIA EVDAR VVREVCSKYF YDQCPAVAGF GPIEQLPDYN RIRSGMFWLR F

UniProtKB: Cytochrome b-c1 complex subunit 1, mitochondrial

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Macromolecule #2: Cytochrome b-c1 complex subunit 2, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 2, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 45.15175 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString: AGVPPHPQDL EFTRLPNGLV IASLENYAPA SRIGLFIKAG SRYENSNNLG TSHLLRLASS LTTKGASSFK ITRGIEAVGG KLSVTSTRE NMAYTVECLR DDVDILMEFL LNVTTAPEFR RWEVAALQPQ LRIDKAVALQ NPQAHVIENL HAAAYRNALA N SLYCPDYR ...String:
AGVPPHPQDL EFTRLPNGLV IASLENYAPA SRIGLFIKAG SRYENSNNLG TSHLLRLASS LTTKGASSFK ITRGIEAVGG KLSVTSTRE NMAYTVECLR DDVDILMEFL LNVTTAPEFR RWEVAALQPQ LRIDKAVALQ NPQAHVIENL HAAAYRNALA N SLYCPDYR IGKVTPVELH DYVQNHFTSA RMALIGLGVS HPVLKQVAEQ FLNIRGGLGL SGAKAKYHGG EIREQNGDSL VH AALVAES AAIGSAEANA FSVLQHVLGA GPHVKRGSNA TSSLYQAVAK GVHQPFDVSA FNASYSDSGL FGFYTISQAA SAG DVIKAA YNQVKTIAQG NLSNPDVQAA KNKLKAGYLM SVESSEGFLD EVGSQALAAG SYTPPSTVLQ QIDAVADADV INAA KKFVS GRKSMAASGN LGHTPFIDEL

UniProtKB: Cytochrome b-c1 complex subunit 2, mitochondrial

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Macromolecule #3: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 42.489145 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString: TNIRKSHPLM KIVNNAFIDL PAPSNISSWW NFGSLLGICL ILQILTGLFL AMHYTSDTTT AFSSVTHICR DVNYGWIIRY MHANGASMF FICLYMHVGR GLYYGSYTFL ETWNIGVILL LTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNL V EWIWGGFS ...String:
TNIRKSHPLM KIVNNAFIDL PAPSNISSWW NFGSLLGICL ILQILTGLFL AMHYTSDTTT AFSSVTHICR DVNYGWIIRY MHANGASMF FICLYMHVGR GLYYGSYTFL ETWNIGVILL LTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNL V EWIWGGFS VDKATLTRFF AFHFILPFII MAIAMVHLLF LHETGSNNPT GISSDVDKIP FHPYYTIKDI LGALLLILAL ML LVLFAPD LLGDPDNYTP ANPLNTPPHI KPEWYFLFAY AILRSIPNKL GGVLALAFSI LILALIPLLH TSKQRSMMFR PLS QCLFWA LVADLLTLTW IGGQPVEHPY ITIGQLASVL YFLLILVLMP TAGTIENKLL KW

UniProtKB: Cytochrome b

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Macromolecule #4: Cytochrome c1, heme protein, mitochondrial

MacromoleculeName: Cytochrome c1, heme protein, mitochondrial / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 27.323277 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString: SDLELHPPSY PWSHRGLLSS LDHTSIRRGF QVYKQVCSSC HSMDYVAYRH LVGVCYTEDE AKALAEEVEV QDGPNEDGEM FMRPGKLSD YFPKPYPNPE AARAANNGAL PPDLSYIVRA RHGGEDYVFS LLTGYCEPPT GVSLREGLYF NPYFPGQAIG M APPIYNEV ...String:
SDLELHPPSY PWSHRGLLSS LDHTSIRRGF QVYKQVCSSC HSMDYVAYRH LVGVCYTEDE AKALAEEVEV QDGPNEDGEM FMRPGKLSD YFPKPYPNPE AARAANNGAL PPDLSYIVRA RHGGEDYVFS LLTGYCEPPT GVSLREGLYF NPYFPGQAIG M APPIYNEV LEFDDGTPAT MSQVAKDVCT FLRWAAEPEH DHRKRMGLKM LLMMGLLLPL VYAMKRHKWS VLKSRKLAYR PP K

UniProtKB: Cytochrome c1, heme protein, mitochondrial

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Macromolecule #5: Cytochrome b-c1 complex subunit Rieske, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske, mitochondrial / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 21.64058 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString: SHTDIKVPDF SDYRRPEVLD STKSSKESSE ARKGFSYLVT ATTTVGVAYA AKNVVSQFVS SMSASADVLA MSKIEIKLSD IPEGKNMAF KWRGKPLFVR HRTKKEIDQE AAVEVSQLRD PQHDLERVKK PEWVILIGVC THLGCVPIAN AGDFGGYYCP C HGSHYDAS ...String:
SHTDIKVPDF SDYRRPEVLD STKSSKESSE ARKGFSYLVT ATTTVGVAYA AKNVVSQFVS SMSASADVLA MSKIEIKLSD IPEGKNMAF KWRGKPLFVR HRTKKEIDQE AAVEVSQLRD PQHDLERVKK PEWVILIGVC THLGCVPIAN AGDFGGYYCP C HGSHYDAS GRIRKGPAPL NLEVPSYEFT SDDMVIVG

UniProtKB: Cytochrome b-c1 complex subunit Rieske, mitochondrial

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Macromolecule #6: Cytochrome b-c1 complex subunit 7

MacromoleculeName: Cytochrome b-c1 complex subunit 7 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 12.917674 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString:
VSASSRWLEG IRKWYYNAAG FNKLGLMRDD TIHENDDVKE AIRRLPENLY DDRVFRIKRA LDLSMRQQIL PKEQWTKYEE DKSYLEPYL KEVIRERKER EEWAKK

UniProtKB: Cytochrome b-c1 complex subunit 7

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Macromolecule #7: Cytochrome b-c1 complex subunit 8

MacromoleculeName: Cytochrome b-c1 complex subunit 8 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 8.856277 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString:
GRQFGHLTRV RHVITYSLSP FEQRAFPHYF SKGIPNVLRR TRACILRVAP PFVAFYLVYT WGTQEFEKSK RKNPA

UniProtKB: Cytochrome b-c1 complex subunit 8

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Macromolecule #8: Cytochrome b-c1 complex subunit 6, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 6, mitochondrial / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 7.886885 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString:
ELVDPLTTVR EQCEQLEKCV KARERLELCD ERVSSRSQTE EDCTEELLDF LHARDHCVAH KLFNSLK

UniProtKB: Cytochrome b-c1 complex subunit 6, mitochondrial

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Macromolecule #9: Cytochrome b-c1 complex subunit 9

MacromoleculeName: Cytochrome b-c1 complex subunit 9 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 5.824802 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString:
MLSVAARSGP FAPVLSATSR GVAGALRPLV QAAVPATSES PVLDLKRSVL CRESLRG

UniProtKB: Cytochrome b-c1 complex subunit Rieske, mitochondrial

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Macromolecule #10: Cytochrome b-c1 complex subunit 9

MacromoleculeName: Cytochrome b-c1 complex subunit 9 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 7.080131 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString:
VAPTLTARLY SLLFRRTSTF ALTIVVGALF FERAFDQGAD AIYEHINEGK LWKHIKHKYE N

UniProtKB: Cytochrome b-c1 complex subunit 9

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Macromolecule #11: Cytochrome b-c1 complex subunit 10

MacromoleculeName: Cytochrome b-c1 complex subunit 10 / type: protein_or_peptide / ID: 11 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 5.978972 KDa
Recombinant expressionOrganism: Bos taurus (domestic cattle)
SequenceString:
LTRFLGPRYR QLARNWVPTA QLWGAVGAVG LVWATDSRLI LDWVPYINGK FK

UniProtKB: Cytochrome b-c1 complex subunit 10

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Macromolecule #12: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 12 / Number of copies: 4 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

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Macromolecule #13: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 13 / Number of copies: 2 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C

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Macromolecule #14: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 14 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 30421492
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionAlgorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 2.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.7) / Number images used: 135149
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

1sqb


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9w2y:
Cryo-EM structure of complex III on the bovine heart submitochondrial particles, III-2

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