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- EMDB-4481: Complex III2 focused refinement from Ovine respiratory supercompl... -

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Basic information

Entry
Database: EMDB / ID: EMD-4481
TitleComplex III2 focused refinement from Ovine respiratory supercomplex I+III2
Map dataFocused refinement around complex III2 from ovine mitochondrial supercomplex I III2
Sample
  • Complex: Ovine mitochondrial SC I+III2
    • Protein or peptide: x 10 types
  • Ligand: x 6 types
Function / homology
Function and homology information


respiratory chain complex III / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respirasome / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity ...respiratory chain complex III / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respirasome / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / mitochondrial inner membrane / electron transfer activity / membrane => GO:0016020 / ubiquitin protein ligase binding / heme binding / proteolysis / nucleoplasm / metal ion binding
Similarity search - Function
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 ...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 9 / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / 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 / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / 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] iron-sulphur domain / Rieske [2Fe-2S] 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 b-c1 complex subunit 6 / Cytochrome b / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome b-c1 complex subunit 7 / Complex III subunit 9 / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit 6 / cytochrome c1, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial
Similarity search - Component
Biological speciesOvis aries (sheep) / Sheep (sheep)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsLetts JA / Sazanov LA
Funding support Austria, 1 items
OrganizationGrant numberCountry
European Research Council701309 Austria
CitationJournal: Mol Cell / Year: 2019
Title: Structures of Respiratory Supercomplex I+III Reveal Functional and Conformational Crosstalk.
Authors: James A Letts / Karol Fiedorczuk / Gianluca Degliesposti / Mark Skehel / Leonid A Sazanov /
Abstract: The mitochondrial electron transport chain complexes are organized into supercomplexes (SCs) of defined stoichiometry, which have been proposed to regulate electron flux via substrate channeling. We ...The mitochondrial electron transport chain complexes are organized into supercomplexes (SCs) of defined stoichiometry, which have been proposed to regulate electron flux via substrate channeling. We demonstrate that CoQ trapping in the isolated SC I+III limits complex (C)I turnover, arguing against channeling. The SC structure, resolved at up to 3.8 Å in four distinct states, suggests that CoQ oxidation may be rate limiting because of unequal access of CoQ to the active sites of CIII. CI shows a transition between "closed" and "open" conformations, accompanied by the striking rotation of a key transmembrane helix. Furthermore, the state of CI affects the conformational flexibility within CIII, demonstrating crosstalk between the enzymes. CoQ was identified at only three of the four binding sites in CIII, suggesting that interaction with CI disrupts CIII symmetry in a functionally relevant manner. Together, these observations indicate a more nuanced functional role for the SCs.
History
DepositionDec 18, 2018-
Header (metadata) releaseAug 21, 2019-
Map releaseAug 21, 2019-
UpdateNov 25, 2020-
Current statusNov 25, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.14
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.14
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6q9e
  • Surface level: 0.14
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4481.png

Downloads & links

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Map

FileDownload / File: emd_4481.map.gz / Format: CCP4 / Size: 184 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFocused refinement around complex III2 from ovine mitochondrial supercomplex I III2
Voxel sizeX=Y=Z: 1.4 Å
Density
Contour LevelBy AUTHOR: 0.14 / Movie #1: 0.14
Minimum - Maximum-0.32649752 - 0.7996147
Average (Standard dev.)-0.00001627164 (±0.017880779)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions364364364
Spacing364364364
CellA=B=C: 509.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.41.41.4
M x/y/z364364364
origin x/y/z0.0000.0000.000
length x/y/z509.600509.600509.600
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS364364364
D min/max/mean-0.3260.800-0.000

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Supplemental data

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Mask #1

Fileemd_4481_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Focused refinement around complex III2 from ovine mitochondrial...

Fileemd_4481_half_map_1.map
AnnotationFocused refinement around complex III2 from ovine mitochondrial supercomplex I III2. Half map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Focused refinement around complex III2 from ovine mitochondrial...

Fileemd_4481_half_map_2.map
AnnotationFocused refinement around complex III2 from ovine mitochondrial supercomplex I III2. Half map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Ovine mitochondrial SC I+III2

EntireName: Ovine mitochondrial SC I+III2
Components
  • Complex: Ovine mitochondrial SC I+III2
    • Protein or peptide: Ubiquinol-cytochrome c reductase core protein 1
    • Protein or peptide: Ubiquinol-cytochrome c reductase core protein 2
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome c1
    • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 7
    • Protein or peptide: Ubiquinol-cytochrome c reductase complex III subunit VII
    • Protein or peptide: Cytochrome b-c1 complex subunit 6
    • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
    • Protein or peptide: Ubiquinol-cytochrome c reductase, complex III subunit X
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE
  • Ligand: CARDIOLIPIN
  • Ligand: UBIQUINONE-10Coenzyme Q10
  • Ligand: HEME C
  • Ligand: FE2/S2 (INORGANIC) CLUSTER

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Supramolecule #1: Ovine mitochondrial SC I+III2

SupramoleculeName: Ovine mitochondrial SC I+III2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#10
Details: Complex III2 focused refinement from ovine respiratory SC I+III2
Source (natural)Organism: Ovis aries (sheep) / Organ: Heart / Tissue: Cardiac / Organelle: Mitochondria / Location in cell: Mitochondrial inner membrane
Molecular weightTheoretical: 1.4 MDa

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Macromolecule #1: Ubiquinol-cytochrome c reductase core protein 1

MacromoleculeName: Ubiquinol-cytochrome c reductase core protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 49.385414 KDa
SequenceString: TATYAQALQS VPETQVSQLD NGLRVASEQS SQPTCTVGVW IDAGSRYETE KNNGAGYFVE HLAFKGTKNR PGNALEKEVE SMGAHLNAY STREHTAYYI KALSKDLPKA VELLADIVQN CSLEDSQIEK ERDVILQELQ ENDTSMRDVV FNYLHATAFQ G TPLAQSVE ...String:
TATYAQALQS VPETQVSQLD NGLRVASEQS SQPTCTVGVW IDAGSRYETE KNNGAGYFVE HLAFKGTKNR PGNALEKEVE SMGAHLNAY STREHTAYYI KALSKDLPKA VELLADIVQN CSLEDSQIEK ERDVILQELQ ENDTSMRDVV FNYLHATAFQ G TPLAQSVE GPSENVRKLS RADLTEYLSR HYKAPRMVLA AAGGLEHRQL LDLAQKHFSG LSGTYDEDAV PTLTPCRFTG SE IRHREDG LPLAHVAIAV EGPGWANPDN VALQVANAII GHYDCTYGGG MHLSSPLASV AVTNKLCQSF QTFNICYADT GLL GAHFVC DHMSIDDMMF VLQGQWMRLC TSATESEVVR GKNLLRNALV SHLDGTTPVC EDIGRSLLTY GRRIPLAEWE SRIA EVDAR VVREVCSKYF YDQCPAVAGF GPIEQLPDYN RIRSGMFWLR F

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Macromolecule #2: Ubiquinol-cytochrome c reductase core protein 2

MacromoleculeName: Ubiquinol-cytochrome c reductase core protein 2 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 46.655531 KDa
SequenceString: SLKVAPKAKA TAAPAGVPQH PQDLEFTRLP NGLVIASLEN YAPASRIGLF IKAGSRYENF NNLGTSHLLR LASSLTTKGA SSFKITRGI EAVGGKLSVT STRENMAYTV ECLRDDVDIL MEFLLNVTTA PEFRRWEVAA LQSQLRIDKA VAFQNPQAHV I ENLHAAAY ...String:
SLKVAPKAKA TAAPAGVPQH PQDLEFTRLP NGLVIASLEN YAPASRIGLF IKAGSRYENF NNLGTSHLLR LASSLTTKGA SSFKITRGI EAVGGKLSVT STRENMAYTV ECLRDDVDIL MEFLLNVTTA PEFRRWEVAA LQSQLRIDKA VAFQNPQAHV I ENLHAAAY RNALANSLYC PDYRIGKVTP DELHDYVQNH FTSARMALIG LGVSHPVLKQ VAEQFLNIRG GLGLSGAKAK YR GGEIREQ NGDSLVHAAL VAESAAIGSA EANAFSVLQH VLGAGPHVKR GSNATSSLYQ AVAKGVHQPF DVSAFNASYS DSG LFGFYT ISQAASAGDV IKAAYNQVKT IAQGNLSNPD VQAAKNKLKA GYLMSVESSE GFLDEVGCQA LAAGSYTPPS TVLQ QIDAV ADADVINAAK KFVSGRKSMA ASGNLGHTPF IDEL

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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: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 42.87784 KDa
SequenceString: MINIRKTHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTPDTT TAFSSVTHIC RDVNYGWIIR YMHANGASM FFICLFMHVG RGLYYGSYTF LETWNIGVIL LFATMATAFM GYVLPWGQMS FWGATVITNL LSAIPYIGTN L VEWIWGGF ...String:
MINIRKTHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTPDTT TAFSSVTHIC RDVNYGWIIR YMHANGASM FFICLFMHVG RGLYYGSYTF LETWNIGVIL LFATMATAFM GYVLPWGQMS FWGATVITNL LSAIPYIGTN L VEWIWGGF SVDKATLTRF FAFHFIFPFI IAALAMVHLL FLHETGSNNP TGIPSDTDKI PFHPYYTIKD ILGAILLILI LM LLVLFTP DLLGDPDNYT PANPLNTPPH IKPEWYFLFA YAILRSIPNK LGGVLALVLS ILVLVIMPLL HTSKQRSMMF RPI SQCMFW ILVADLLTLT WIGGQPVEHP YIIIGQLASI MYFLIILVMM PVASIIENNL LKW

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Macromolecule #4: Cytochrome c1

MacromoleculeName: Cytochrome c1 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 27.322316 KDa
SequenceString: SDLELHPPSY PWSHRGLLSS LDHTSIRRGF QVYKQVCSSC HSMDYVAYRH LVGVCYTEDE AKALAEEVEV QDGPNEDGEM FMRPGKLSD YFPKPYPNPE AARAANNGAL PPDLSYIVRA RHGGEDYVFS LLTGYCEPPR VSLREGLYFN PYFPGQAIGM A PPIYNEVL ...String:
SDLELHPPSY PWSHRGLLSS LDHTSIRRGF QVYKQVCSSC HSMDYVAYRH LVGVCYTEDE AKALAEEVEV QDGPNEDGEM FMRPGKLSD YFPKPYPNPE AARAANNGAL PPDLSYIVRA RHGGEDYVFS LLTGYCEPPR VSLREGLYFN PYFPGQAIGM A PPIYNEVL EFDDGTPATM SQVAKDVCTF LRWAAEPEHD HRKRMGLKML LMMGLLLPLV YAMKRHKWSV LKSRKLAYRP PK

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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: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 21.654607 KDa
SequenceString: SHTDIKVPDF SDYRRPEVLD STKSSKESSE ARKGFSYLIT ATTTVGVAYA AKNVVSQFVS SMSASADVLA MSKIEIKLSD IPEGKNMAF KWRGKPLFVR HRTKKEIDQE AAVEVSQLRD PQHDLERVKK PEWVILIGVC THLGCVPIAN AGDFGGYYCP C HGSHYDAS ...String:
SHTDIKVPDF SDYRRPEVLD STKSSKESSE ARKGFSYLIT ATTTVGVAYA AKNVVSQFVS SMSASADVLA MSKIEIKLSD IPEGKNMAF KWRGKPLFVR HRTKKEIDQE AAVEVSQLRD PQHDLERVKK PEWVILIGVC THLGCVPIAN AGDFGGYYCP C HGSHYDAS GRIRKGPAPL NLEVPSYEFT SDDMVIVG

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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: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 13.432314 KDa
SequenceString:
AGRPAVSASS KWLEGIRKWY YNAAGFNKLG LMRDDTIHEN DDVKEAIRRL PENLYNDRVF RIKRALDLSM RQQILPKEQW TKYEEDKFY LEPYLKEVIR ERKEREEWTK K

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Macromolecule #7: Ubiquinol-cytochrome c reductase complex III subunit VII

MacromoleculeName: Ubiquinol-cytochrome c reductase complex III subunit VII
type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 9.606067 KDa
SequenceString:
GRQFGHLTRV RHVITYSLSP FEQRAFPHYF SKGIPNVLRR TRACILRVAP PFVVFYLVYT WGTQEFEKSK RKNPAAYEND K

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Macromolecule #8: Cytochrome b-c1 complex subunit 6

MacromoleculeName: Cytochrome b-c1 complex subunit 6 / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 9.223133 KDa
SequenceString:
GDPKEEEEEE EELVDPLTTV REQCEQLEKC VKARERLELC DERVSSRSQT EEDCTEELFD FLHARDHCVA HKLFNSLK

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Macromolecule #9: Cytochrome b-c1 complex subunit Rieske, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske, mitochondrial / type: protein_or_peptide / ID: 9 / Details: Modeled as poly-alanine due to poor density. / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 2.826475 KDa
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)

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Macromolecule #10: Ubiquinol-cytochrome c reductase, complex III subunit X

MacromoleculeName: Ubiquinol-cytochrome c reductase, complex III subunit X
type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sheep (sheep) / Organ: Heart / Tissue: Cardiac
Molecular weightTheoretical: 7.310372 KDa
SequenceString:
AAPTLTARLY SLLFRRTSTF ALTIVVGALF FERAFDQGAD AIYEHINEGK LWKHIKHKYE NKE

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Macromolecule #11: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 11 / Number of copies: 4 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

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Macromolecule #12: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE / type: ligand / ID: 12 / Number of copies: 4 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da

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Macromolecule #13: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 13 / Number of copies: 5 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #14: UBIQUINONE-10

MacromoleculeName: UBIQUINONE-10 / type: ligand / ID: 14 / Number of copies: 3 / Formula: U10
Molecular weightTheoretical: 863.343 Da
Chemical component information

ChemComp-U10:
UBIQUINONE-10 / Coenzyme Q10

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Macromolecule #15: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 15 / Number of copies: 2 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C / Heme C

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Macromolecule #16: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 16 / Number of copies: 2 / Formula: FES
Molecular weightTheoretical: 175.82 Da
Chemical component information

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur 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

Concentration2 mg/mL
BufferpH: 7.4
Component:
ConcentrationFormulaName
0.25 MNaClSodium chloridesodium chloride
0.02 MHEPES
0.02 %Brij-35

Details: 250 mM NaCl, 20 mM HEPES, pH 7.7, 0.02% Brij-35
VitrificationCryogen name: PROPANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
Details: blotting for 30 seconds at 4 degrees Celsius, 95% humidity and flash freezing.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELDBright-field microscopy
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Number grids imaged: 1 / Number real images: 1854 / Average exposure time: 2.0 sec. / Average electron dose: 51.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 400000
CTF correctionSoftware - Name: Gctf
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

5lnk

Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2)
Final 3D classificationNumber classes: 3 / Software - Name: RELION (ver. 2)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2)
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2) / Number images used: 102314
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

1ppj

RefinementSpace: REAL / Protocol: OTHER / Overall B value: 90
Output model

PDB-6q9e:
Complex III2 focused refinement from Ovine respiratory supercomplex I+III2

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