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- EMDB-15998: Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex... -

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Entry
Database: EMDB / ID: EMD-15998
TitleCryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (CI peripheral tip)
Map data
Sample
  • Complex: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CI peripheral tip)
    • Protein or peptide: x 8 types
  • Ligand: x 5 types
Function / homology
Function and homology information


cold acclimation / photorespiration / response to osmotic stress / cobalt ion binding / plastid / respiratory chain complex I / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial electron transport, NADH to ubiquinone / NADH dehydrogenase (ubiquinone) activity ...cold acclimation / photorespiration / response to osmotic stress / cobalt ion binding / plastid / respiratory chain complex I / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial electron transport, NADH to ubiquinone / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / chloroplast / mitochondrial membrane / 2 iron, 2 sulfur cluster binding / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / mitochondrion / zinc ion binding / metal ion binding / plasma membrane / cytosol
Similarity search - Function
NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Soluble ligand binding domain / SLBB domain / Zinc finger, CHCC-type / Zinc-finger domain / NDUFA6, LYR domain / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 ...NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial / Soluble ligand binding domain / SLBB domain / Zinc finger, CHCC-type / Zinc-finger domain / NDUFA6, LYR domain / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH-quinone oxidoreductase, chain G, C-terminal / NADH-ubiquinone oxidoreductase subunit G, C-terminal / NADH-quinone oxidoreductase, chain I / NADH:ubiquinone oxidoreductase, subunit G / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. / NADH ubiquinone oxidoreductase, F subunit / 2Fe-2S iron-sulfur cluster binding domain / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. / Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. / NuoE domain / NADH-quinone oxidoreductase subunit E-like / Thioredoxin-like [2Fe-2S] ferredoxin / NADH-quinone oxidoreductase subunit E, N-terminal / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / His(Cys)3-ligated-type [4Fe-4S] domain profile. / NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site / Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain / NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily / NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily / Respiratory-chain NADH dehydrogenase 51 Kd subunit / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / NADH-ubiquinone oxidoreductase-F iron-sulfur binding region / Molybdopterin oxidoreductase, 4Fe-4S domain / Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile. / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / Ribosomal protein/NADH dehydrogenase domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / Mitochondrial ribosomal protein L51 / S25 / CI-B8 domain / 4Fe-4S dicluster domain / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain / Thioredoxin-like superfamily
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress) / thale cress (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.03 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_15998.png

Downloads & links

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Map

FileDownload / File: emd_15998.map.gz / Format: CCP4 / Size: 36.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesX (Sec.)Y (Row.)Z (Col.)
0.57 Å/pix.
x 184 pix.
= 105.432 Å		0.57 Å/pix.
x 255 pix.
= 146.115 Å		0.57 Å/pix.
x 204 pix.
= 116.892 Å

Surface

Projections

Slices (1/3)

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Slices (2/3)

Images are generated by Spider.

generated in cubic-lattice coordinate

Voxel sizeX=Y=Z: 0.573 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.8
Minimum - Maximum-8.949057 - 14.342239
Average (Standard dev.)1.2562527e-12 (±0.43444473)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin91350188
Dimensions255204184
Spacing184255204
CellA: 105.432 Å / B: 146.115 Å / C: 116.892006 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_15998_additional_1.map
Projections & Slices
AxesZYX

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Half map: #2

Fileemd_15998_half_map_1.map
Projections & Slices
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Histogram

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Half map: #1

Fileemd_15998_half_map_2.map
Projections & Slices
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Sample components

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Entire : Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CI periph...

EntireName: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CI peripheral tip)
Components
  • Complex: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CI peripheral tip)
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: FLAVIN MONONUCLEOTIDE
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: ZINC ION
  • Ligand: water

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Supramolecule #1: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CI periph...

SupramoleculeName: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CI peripheral tip)
type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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Macromolecule #1: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 28.423607 KDa
SequenceString: MLARLAAKRL LEIRQVFRQP TSQVTRSLST ALNYHLDSPD NKPDLPWEFS EANQSKVKEI LSYYPSNYKQ SAVIPLLDLA QQQNGGWLP VSAMNAVAKV IEVAPIRVYE VATFYSMFNR AKVGKYHLLV CGTTPCMIRG SRDIESALLD HLGVKRGEVT K DGLFSVGE ...String:
MLARLAAKRL LEIRQVFRQP TSQVTRSLST ALNYHLDSPD NKPDLPWEFS EANQSKVKEI LSYYPSNYKQ SAVIPLLDLA QQQNGGWLP VSAMNAVAKV IEVAPIRVYE VATFYSMFNR AKVGKYHLLV CGTTPCMIRG SRDIESALLD HLGVKRGEVT K DGLFSVGE MECMGCCVNA PMITVADYSN GSEGYTYNYF EDVTPEKVVE IVEKLRKGEK PPHGTQNPKR IKCGPEGGNK TL LGEPKPP QFRDLDAC

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Macromolecule #2: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 53.522418 KDa
SequenceString: MAPVRGILGL QRAVSIWKES NRLTPALRSF STQAASTSTT PQPPPPPPPP EKTHFGGLKD EDRIFTNLYG LHDPFLKGAM KRGDWHRTK DLVLKGTDWI VNEMKKSGLR GRGGAGFPSG LKWSFMPKVS DGRPSYLVVN ADESEPGTCK DREIMRHDPH K LLEGCLIA ...String:
MAPVRGILGL QRAVSIWKES NRLTPALRSF STQAASTSTT PQPPPPPPPP EKTHFGGLKD EDRIFTNLYG LHDPFLKGAM KRGDWHRTK DLVLKGTDWI VNEMKKSGLR GRGGAGFPSG LKWSFMPKVS DGRPSYLVVN ADESEPGTCK DREIMRHDPH K LLEGCLIA GVGMRASAAY IYIRGEYVNE RLNLEKARRE AYAAGLLGKN ACGSGYDFEV YIHFGAGAYI CGEETALLES LE GKQGKPR LKPPFPANAG LYGCPTTVTN VETVAVSPTI LRRGPEWFSS FGRKNNAGTK LFCISGHVNK PCTVEEEMSI PLK ELIERH CGGVRGGWDN LLAIIPGGSS VPLIPKNICE DVLMDFDALK AVQSGLGTAA VIVMDKSTDV VDAIARLSYF YKHE SCGQC TPCREGTGWL WMIMERMKVG NAKLEEIDML QEVTKQIEGH TICALGDAAA WPVQGLIRHF RPELERRIRE RAERE LLQA AA

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Macromolecule #3: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 81.619367 KDa
SequenceString: MGLGILASRT IRPASRLLQS QTSNFFLRTI VSKPELQSPE SAAVSEPEPP TQILPPRNPV GGARVHFSNP EDAIEVFVDG YAVKVPKGF TVLQACEVAG VDIPRFCYHS RLSIAGNCRM CLVEVEKSPK PVASCAMPAL PGMKIKTDTP IAKKAREGVM E FLLMNHPL ...String:
MGLGILASRT IRPASRLLQS QTSNFFLRTI VSKPELQSPE SAAVSEPEPP TQILPPRNPV GGARVHFSNP EDAIEVFVDG YAVKVPKGF TVLQACEVAG VDIPRFCYHS RLSIAGNCRM CLVEVEKSPK PVASCAMPAL PGMKIKTDTP IAKKAREGVM E FLLMNHPL DCPICDQGGE CDLQDQSMAF GSDRGRFTEM KRSVVDKNLG PLVKTVMTRC IQCTRCVRFA SEVAGVQDLG IL GRGSGEE IGTYVEKLMT SELSGNVIDI CPVGALTSKP FAFKARNWEL KATETIDVSD AVGSNIRVDS RGPEVMRIIP RLN EDINEE WISDKTRFCY DGLKRQRLSD PMIRDSDGRF KAVSWRDALA VVGDIIHQVK PDEIVGVAGQ LSDAESMMVL KDFV NRMGS DNVWCEGTAA GVDADLRYSY LMNTSISGLE NADLFLLIGT QPRVEAAMVN ARICKTVRAS NAKVGYVGPP AEFNY DCKH LGTGPDTLKE IAEGRHPFCT ALKNAKNPAI IVGAGLFNRT DKNAILSSVE SIAQANNVVR PDWNGLNFLL QYAAQA AAL DLGLIQQSAK ALESAKFVYL MGADDVNVDK IPKDAFVVYQ GHHGDKAVYR ANVILPASAF TEKEGTYENT EGFTQQT VP AVPTVGDARD DWKIVRALSE VSGVKLPYNS IEGVRSRIKS VAPNLVHTDE REPAAFGPSL KPECKEAMST TPFQTVVE N FYMTNSITRA SKIMAQCSAV LLKKPFV

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Macromolecule #4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: NADH:ubiquinone reductase (H+-translocating)
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 25.536801 KDa
SequenceString: MASILARRSL NTLRARHLVL SGQALQGSHL SRLQSRGISY GSNKDDEEAE QLSKEISKDW NTVFERSINT LFLTEMVRGL SLTLKYFFD PKVTINYPFE KGPLSPRFRG EHALRRYPTG EERCIACKLC EAVCPAQAIT IEAEEREDGS RRTTRYDIDM T KCIYCGFC ...String:
MASILARRSL NTLRARHLVL SGQALQGSHL SRLQSRGISY GSNKDDEEAE QLSKEISKDW NTVFERSINT LFLTEMVRGL SLTLKYFFD PKVTINYPFE KGPLSPRFRG EHALRRYPTG EERCIACKLC EAVCPAQAIT IEAEEREDGS RRTTRYDIDM T KCIYCGFC QEACPVDAIV EGPNFEFATE THEELLYDKE KLLENGDRWE TEIAENLRSE SLYR

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Macromolecule #5: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 17.160445 KDa
SequenceString:
MALCATTQRT IRIAATLRRV ARPFATDAVV ESDYKRGEIG KVSGIPEEHL SRKVIIYSPA RTATQSGSGK LGKWKINFVS TLKWENPLM GWTSTGDPYA NVGDSALAFD SEEAAKSFAE RHGWDYKVKK PNTPLLKVKS YSDNFKWKGN PQPEN

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Macromolecule #6: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 12.251122 KDa
SequenceString:
MASNLLKALI RSQILPSSRR NFSVATTQLG IPTDDLVGNH TAKWMQDRSK KSPMELISEV PPIKVDGRIV ACEGDTNPAL GHPIEFICL DLNEPAICKY CGLRYVQDHH H

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Macromolecule #7: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 10.865765 KDa
SequenceString:
MAWRGSISKS MKELRILLCQ SSPASAPTRT FVEKNYKDLK SLNPKLPILI RECSGVQPQM WARYDMGVER CVNLDGLTEP QILKALENL VKSGATKA

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Macromolecule #8: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 15.102261 KDa
SequenceString:
MAAPFALRKI GVPPNSANLT EARRRVFDFF RAACRSIPTI MDIYNLQDVV APSQLRYAIS AQIRNNAHIT DPKVIDLLIF KGMEELTDI VDHAKQRHHI IGQYVVGEGL VQNTGNKDQG KTDFLKNFYT SNYF

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Macromolecule #9: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 9 / 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 #10: FLAVIN MONONUCLEOTIDE

MacromoleculeName: FLAVIN MONONUCLEOTIDE / type: ligand / ID: 10 / Number of copies: 1 / Formula: FMN
Molecular weightTheoretical: 456.344 Da
Chemical component information

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

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Macromolecule #11: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 11 / Number of copies: 3 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

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Macromolecule #12: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 12 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #13: water

MacromoleculeName: water / type: ligand / ID: 13 / Number of copies: 646 / 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: 2.03 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-8bed:
Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (CI peripheral tip)

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