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- EMDB-16007: Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex... -

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Basic information

Entry
Database: EMDB / ID: EMD-16007
TitleCryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (CIII membrane domain)
Map data
Sample
  • Complex: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CIII membrane domain)
    • Protein or peptide: x 7 types
  • Ligand: x 11 types
Function / homology
Function and homology information


respiratory chain complex III / mitochondrial respiratory chain complex III / vacuole / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / plastid / mitochondrial electron transport, ubiquinol to cytochrome c / respiratory electron transport chain / mitochondrial membrane / 2 iron, 2 sulfur cluster binding ...respiratory chain complex III / mitochondrial respiratory chain complex III / vacuole / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / plastid / mitochondrial electron transport, ubiquinol to cytochrome c / respiratory electron transport chain / mitochondrial membrane / 2 iron, 2 sulfur cluster binding / mitochondrial inner membrane / electron transfer activity / heme binding / mitochondrion / metal ion binding / cytosol
Similarity search - Function
Cytochrome b-c1 complex subunit 8, plants / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex, subunit 6 / 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 ...Cytochrome b-c1 complex subunit 8, plants / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex, subunit 6 / 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. / 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 / 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 / Cytochrome b-c1 complex subunit 6-1, mitochondrial / Cytochrome b-c1 complex subunit Rieske-1, mitochondrial / Cytochrome b-c1 complex subunit 10, mitochondrial / Cytochrome c1 2, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 9, mitochondrial / Cytochrome b-c1 complex subunit 8-1, mitochondrial
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress) / thale cress (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.25 Å
AuthorsKlusch N / Kuehlbrandt W
Funding support Germany, 1 items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: Nat Plants / Year: 2023
Title: Cryo-EM structure of the respiratory I + III supercomplex from Arabidopsis thaliana at 2 Å resolution.
Authors: Niklas Klusch / Maximilian Dreimann / Jennifer Senkler / Nils Rugen / Werner Kühlbrandt / Hans-Peter Braun /
Abstract: Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis ...Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis respiratory supercomplex consisting of complex I and a complex III dimer, with a total of 68 protein subunits and numerous bound cofactors. A complex I-ferredoxin, subunit B14.7 and P9, a newly defined subunit of plant complex I, mediate supercomplex formation. The component complexes stabilize one another, enabling new detailed insights into their structure. We describe (1) an interrupted aqueous passage for proton translocation in the membrane arm of complex I; (2) a new coenzyme A within the carbonic anhydrase module of plant complex I defining a second catalytic centre; and (3) the water structure at the proton exit pathway of complex III with a co-purified ubiquinone in the Q site. We propose that the main role of the plant supercomplex is to stabilize its components in the membrane.
History
DepositionOct 21, 2022-
Header (metadata) releaseJan 11, 2023-
Map releaseJan 11, 2023-
UpdateFeb 1, 2023-
Current statusFeb 1, 2023Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_16007.png

Downloads & links

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Map

FileDownload / File: emd_16007.map.gz / Format: CCP4 / Size: 68.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.573 Å
Density
Contour LevelBy AUTHOR: 0.6
Minimum - Maximum-3.6454554 - 10.97669
Average (Standard dev.)1.10598766e-13 (±0.28790298)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin337198214
Dimensions285249254
Spacing254285249
CellA: 145.542 Å / B: 163.30501 Å / C: 142.677 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_16007_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_16007_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_16007_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CIII memb...

EntireName: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CIII membrane domain)
Components
  • Complex: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CIII membrane domain)
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
    • Protein or peptide: Cytochrome c1 2, heme protein, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 8-1, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 6-1, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 9, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 10, mitochondrial
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE
  • Ligand: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE
  • Ligand: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE
  • Ligand: CARDIOLIPIN
  • Ligand: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: PHOSPHATIDYLETHANOLAMINE
  • Ligand: UBIQUINONE-7Coenzyme Q10
  • Ligand: 2-{[(4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranosyl)oxy]methyl}-4-{[(3beta,9beta,14beta,17beta,25R)-spirost-5-en-3-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside
  • Ligand: water

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Supramolecule #1: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CIII memb...

SupramoleculeName: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CIII membrane domain)
type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: #1-#7
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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Macromolecule #1: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 44.310609 KDa
SequenceString: MTIRNQRFSL LKQPISSTLN QHLVDYPTPS NLSYWWGFGS LAGICLVIQI VTGVFLAMHY TPHVDLAFNS VEHIMRDVEG GWLLRYMHA NGASMFFIVV YLHIFRGLYY ASYSSPREFV WCLGVVIFLL MIVTAFIGYV LPWGQMSFWG ATVITSLASA I PVVGDTIV ...String:
MTIRNQRFSL LKQPISSTLN QHLVDYPTPS NLSYWWGFGS LAGICLVIQI VTGVFLAMHY TPHVDLAFNS VEHIMRDVEG GWLLRYMHA NGASMFFIVV YLHIFRGLYY ASYSSPREFV WCLGVVIFLL MIVTAFIGYV LPWGQMSFWG ATVITSLASA I PVVGDTIV TWLWGGFSVD NATLNRFFSL HYLLPFILVG ASLLHLAALH QYGSNNPLGV HSEMDKIAFY PYFYVKDLVG WV AFAIFFS IWIFYAPNVL GHPDNYIPAN PMSTPPHIVP EWYFLPIYAI LRSIPDKAGG VAAIALVFIC LLALPFFKSM YVR SSSFRP IYQGMFWLLL ADCLLLGWIG CQPVEAPFVT IGQISSLVFF LFFAITPILG RVGRGIPNSY TDETDHT

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Macromolecule #2: Cytochrome b-c1 complex subunit Rieske-1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 29.645584 KDa
SequenceString: MLRVAGRRLF SVSQRSSTAT SFVVSRDHTL SDGGGDSSSA PRSLPSADLS SYHRSLIRGF SSQVLAQGNE IGFGSEVPAT VEAVKTPNS KIVYDDHNHE RYPPGDPSKR AFAYFVLSGG RFVYASVLRL LVLKLIVSMS ASKDVLALAS LEVDLGSIEP G TTVTVKWR ...String:
MLRVAGRRLF SVSQRSSTAT SFVVSRDHTL SDGGGDSSSA PRSLPSADLS SYHRSLIRGF SSQVLAQGNE IGFGSEVPAT VEAVKTPNS KIVYDDHNHE RYPPGDPSKR AFAYFVLSGG RFVYASVLRL LVLKLIVSMS ASKDVLALAS LEVDLGSIEP G TTVTVKWR GKPVFIRRRT EDDIKLANSV DVGSLRDPQE DSVRVKNPEW LVVVGVCTHL GCIPLPNAGD YGGWFCPCHG SH YDISGRI RKGPAPYNLE VPTYSFLEEN KLLIG

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Macromolecule #3: Cytochrome c1 2, heme protein, mitochondrial

MacromoleculeName: Cytochrome c1 2, heme protein, mitochondrial / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 33.728238 KDa
SequenceString: MVGGGVIRQL LRRKLHSQSV ATPVLSWLSS KKANEDAGSA GLRAFALMGA GITGLLSFST VASADEAEHG LECPNYPWPH EGILSSYDH ASIRRGHQVY QQVCASCHSM SLISYRDLVG VAYTEEEAKA MAAEIEVVDG PNDEGEMFTR PGKLSDRLPE P YSNESAAR ...String:
MVGGGVIRQL LRRKLHSQSV ATPVLSWLSS KKANEDAGSA GLRAFALMGA GITGLLSFST VASADEAEHG LECPNYPWPH EGILSSYDH ASIRRGHQVY QQVCASCHSM SLISYRDLVG VAYTEEEAKA MAAEIEVVDG PNDEGEMFTR PGKLSDRLPE P YSNESAAR FANGGAYPPD LSLVTKARHN GQNYVFALLT GYRDPPAGIS IREGLHYNPY FPGGAIAMPK MLNDEAVEYE DG TPATEAQ MGKDVVSFLS WAAEPEMEER KLMGFKWIFL LSLALLQAAY YRRLKWSVLK SRKLVLDVVN

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Macromolecule #4: Cytochrome b-c1 complex subunit 8-1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 8-1, mitochondrial / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 8.517977 KDa
SequenceString:
MGKQPVKLKA VVYALSPFQQ KIMTGLWKDL PEKIHHKVSE NWISATLLVT PVVGTYWYAQ YFKEQEKLEH RF

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Macromolecule #5: Cytochrome b-c1 complex subunit 6-1, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 6-1, mitochondrial / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 7.997315 KDa
SequenceString:
MADDEVVDPK KYLEESCKPK CVKPLLEYQA CVKRIQGDDS GHKHCTGQYF DYWQCIDKCV APKLFAKLK

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Macromolecule #6: Cytochrome b-c1 complex subunit 9, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 9, mitochondrial / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 8.461634 KDa
SequenceString:
MEYAARRNQK GAFEGFYKLI MRRNSVYVTF IIAGAFFGER AVDYGVHKLW ERNNVGKRYE DISVLGQRPV EE

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Macromolecule #7: Cytochrome b-c1 complex subunit 10, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 10, mitochondrial / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 5.980947 KDa
SequenceString:
MAGTSGLLNA VKPKIQTIDI QAAAGWGIAA AAGAIWVVQP FGWIKKTFID PPPTEEK

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Macromolecule #8: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 8 / Number of copies: 6 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

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Macromolecule #9: 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14...

MacromoleculeName: 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE
type: ligand / ID: 9 / Number of copies: 3 / Formula: UQ5
Molecular weightTheoretical: 522.758 Da
Chemical component information

ChemComp-UQ5:
2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE

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Macromolecule #10: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE

MacromoleculeName: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE / type: ligand / ID: 10 / Number of copies: 6 / Formula: 3PH
Molecular weightTheoretical: 704.998 Da
Chemical component information

ChemComp-3PH:
1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE / Phosphatidic acid

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Macromolecule #11: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...

MacromoleculeName: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE
type: ligand / ID: 11 / Number of copies: 4 / Formula: PGT
Molecular weightTheoretical: 751.023 Da
Chemical component information

ChemComp-PGT:
(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipid*YM / Phosphatidylglycerol

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Macromolecule #12: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 12 / Number of copies: 7 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #13: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5...

MacromoleculeName: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE
type: ligand / ID: 13 / Number of copies: 5 / Formula: PC7
Molecular weightTheoretical: 763.1 Da
Chemical component information

ChemComp-PC7:
(7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE / phospholipid*YM / Phosphatidylcholine

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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 / Iron–sulfur cluster

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Macromolecule #15: PHOSPHATIDYLETHANOLAMINE

MacromoleculeName: PHOSPHATIDYLETHANOLAMINE / type: ligand / ID: 15 / Number of copies: 3 / Formula: PTY
Molecular weightTheoretical: 734.039 Da
Chemical component information

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

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Macromolecule #16: UBIQUINONE-7

MacromoleculeName: UBIQUINONE-7 / type: ligand / ID: 16 / Number of copies: 1 / Formula: UQ7
Molecular weightTheoretical: 658.992 Da
Chemical component information

ChemComp-UQ7:
UBIQUINONE-7

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Macromolecule #17: 2-{[(4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranosyl)oxy]methyl...

MacromoleculeName: 2-{[(4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranosyl)oxy]methyl}-4-{[(3beta,9beta,14beta,17beta,25R)-spirost-5-en-3-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside
type: ligand / ID: 17 / Number of copies: 2 / Formula: Q7G
Molecular weightTheoretical: 1.165315 KDa
Chemical component information

ChemComp-Q7G:
2-{[(4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranosyl)oxy]methyl}-4-{[(3beta,9beta,14beta,17beta,25R)-spirost-5-en-3-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside

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Macromolecule #18: water

MacromoleculeName: water / type: ligand / ID: 18 / Number of copies: 744 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER / Water

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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

Concentration0.18 mg/mL
BufferpH: 7.4
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Support film - #0 - Film type ID: 1 / Support film - #0 - Material: CARBON / Support film - #0 - topology: CONTINUOUS / Support film - #1 - Film type ID: 2 / Support film - #1 - Material: GRAPHENE / Support film - #1 - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 70 % / Chamber temperature: 283.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 215000
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1215138
Startup modelType of model: EMDB MAP
EMDB ID:

11878

Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1.3)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.25 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1.3) / Number images used: 213993
FSC plot (resolution estimation)

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Atomic model buiding 1

SoftwareName: Coot (ver. 0.9.5)
RefinementSpace: REAL
Output model

PDB-8bel:
Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (CIII membrane domain)

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