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- EMDB-15999: Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex... -

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Basic information

Entry
Database: EMDB / ID: EMD-15999
TitleCryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (CI peripheral core)
Map data
Sample
  • Complex: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CI peripheral core)
    • Protein or peptide: x 10 types
  • Ligand: x 4 types
Function / homology
Function and homology information


photorespiration / embryo development ending in seed dormancy / cobalt ion binding / plastid / respiratory chain complex I / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial electron transport, NADH to ubiquinone / acyl carrier activity / mitochondrial respiratory chain complex I assembly ...photorespiration / embryo development ending in seed dormancy / cobalt ion binding / plastid / respiratory chain complex I / NADH:ubiquinone reductase (H+-translocating) / mitochondrial respiratory chain complex I / mitochondrial electron transport, NADH to ubiquinone / acyl carrier activity / mitochondrial respiratory chain complex I assembly / NADH dehydrogenase (ubiquinone) activity / quinone binding / respiratory electron transport chain / mitochondrial membrane / NAD binding / 4 iron, 4 sulfur cluster binding / mitochondrial matrix / mitochondrion / zinc ion binding / extracellular region / metal ion binding / nucleus / plasma membrane / cytosol
Similarity search - Function
GRIM-19 / GRIM-19 protein / NDUFA6, LYR domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit ...GRIM-19 / GRIM-19 protein / NDUFA6, LYR domain / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / ETC complex I subunit conserved region / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH dehydrogenase, subunit C / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / NAD-dependent epimerase/dehydratase / NAD dependent epimerase/dehydratase family / NADH:ubiquinone oxidoreductase-like, 20kDa subunit / NADH ubiquinone oxidoreductase, 20 Kd subunit / [NiFe]-hydrogenase, large subunit / Acyl carrier protein (ACP) / 4Fe-4S dicluster domain / Phosphopantetheine attachment site / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / Phosphopantetheine attachment 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 / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
NADH dehydrogenase [ubiquinone] iron-sulfur protein 2 / Acyl carrier protein 2, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial / NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A / NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 / Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 / Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress) / thale cress (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.04 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_15999.png

Downloads & links

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Map

FileDownload / File: emd_15999.map.gz / Format: CCP4 / Size: 43.8 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 223 pix.
= 127.779 Å		0.57 Å/pix.
x 233 pix.
= 133.509 Å		0.57 Å/pix.
x 221 pix.
= 126.633 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

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-8.29981 - 17.741827
Average (Standard dev.)-3.2807138e-12 (±0.4202595)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin155278230
Dimensions233221223
Spacing223233221
CellA: 127.779 Å / B: 133.509 Å / C: 126.633 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_15999_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_15999_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_15999_half_map_2.map
Projections & Slices
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Slices (1/2)
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Histogram (log scale)

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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 core)
Components
  • Complex: Mitochondrial Arabidopsis thaliana I+III2 supercomplex (CI peripheral core)
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3
    • Protein or peptide: NADH dehydrogenase subunit 7
    • Protein or peptide: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8-A, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
    • Protein or peptide: Acyl carrier protein 2, mitochondrial
    • Protein or peptide: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, mitochondrial
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
    • Protein or peptide: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A
    • Protein or peptide: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
  • 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 core)
type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: #1-#10
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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Macromolecule #1: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, 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: 24.071949 KDa
SequenceString: MAMITRNTAT RLPLLLQSQR AVAAASVSHL HTSLPALSPS TSPTSYTRPG PPSTSPPPPG LSKAAEFVIS KVDDLMNWAR TGSIWPMTF GLACCAVEMM HTGAARYDLD RFGIIFRPSP RQSDCMIVAG TLTNKMAPAL RKVYDQMPEP RWVISMGSCA N GGGYYHYS ...String:
MAMITRNTAT RLPLLLQSQR AVAAASVSHL HTSLPALSPS TSPTSYTRPG PPSTSPPPPG LSKAAEFVIS KVDDLMNWAR TGSIWPMTF GLACCAVEMM HTGAARYDLD RFGIIFRPSP RQSDCMIVAG TLTNKMAPAL RKVYDQMPEP RWVISMGSCA N GGGYYHYS YSVVRGCDRI VPVDIYVPGC PPTAEALLYG LLQLQKKINR RKDFLHWWNK

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Macromolecule #2: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3

MacromoleculeName: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 / 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: 22.91091 KDa
SequenceString:
MDNQFIFKYS WETLPKKWVK KMERSEHGNR FDTNTDYLFQ LLCFLKLHTY TRVQVLIDIC GVDYPSRKRR FEVVYNLLST RYNSRIRVQ TSADEVTRIS SVVSLFPSAG WWEREVWDMF GVSFINHPDL RRILTDYGFE GHPLRKDFPL SGYVQVRYDD P EKRVVSEP IEMTQEFRYF DFASPWEQRS DG

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Macromolecule #3: NADH dehydrogenase subunit 7

MacromoleculeName: NADH dehydrogenase subunit 7 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 45.036844 KDa
SequenceString: MTTRKRQIKN FTLNFGPQHP AAHGVLRLVL EMNGEVVERA EPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMAQEH AYSLAVEKL LNCEVPLRAQ YIRVLFCEIT RILNHLLALT THAMDVGALT PFLWAFEERE KLLEFYERVS GARMHASFIR P GGVAQDLP ...String:
MTTRKRQIKN FTLNFGPQHP AAHGVLRLVL EMNGEVVERA EPHIGLLHRG TEKLIEYKTY LQALPYFDRL DYVSMMAQEH AYSLAVEKL LNCEVPLRAQ YIRVLFCEIT RILNHLLALT THAMDVGALT PFLWAFEERE KLLEFYERVS GARMHASFIR P GGVAQDLP LGLCRDIDSF TQQFASRIDE LEEMLTGNRI WKQRLVDIGT VTAQQAKDWG FSGVMLRGSG VCWDLRRAAP YD VYDQLDF DVPVGTRGDC YDRYCIRIEE MRQSLRIIVQ CLNQMPSGMI KADDRKLCPP SRCRMKLSME SLIHHFELYT EGF SVPASS TYTAVEAPKG EFGVFLVSNG SNRPYRCKIR APGFAHSQGL DFMSKHHMLA DVVTIIGTQD IVFGEVDR

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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] 1 alpha subcomplex subunit 9, mit...

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 43.988652 KDa
SequenceString: MQVVSRRLVQ RPLVGGASIY SSSSLRSLYG VSNHLNGTDN CRYSSSLATK GVGHLARKGT GGRSSVSGIV ATVFGATGFL GRYLVQQLA KMGSQVLVPF RGSEDSPRHL KLMGDLGQVV PMKFDPRDED SIKAVMAKAN VVINLIGREY ETRNFSFEDA N HHIAEKLA ...String:
MQVVSRRLVQ RPLVGGASIY SSSSLRSLYG VSNHLNGTDN CRYSSSLATK GVGHLARKGT GGRSSVSGIV ATVFGATGFL GRYLVQQLA KMGSQVLVPF RGSEDSPRHL KLMGDLGQVV PMKFDPRDED SIKAVMAKAN VVINLIGREY ETRNFSFEDA N HHIAEKLA LVAKEHGGIM RYIQVSCLGA SVSSPSRMLR AKAAAEEAVL NALPEATIMR PATMIGTEDR ILNPWSMFVK KY GFLPLIG GGTTKFQPVY VVDVAAAIVA ALKDDGSSMG KTYELGGPDV FTTHELAEIM YDMIREWPRY VKLPFPIAKA MAA PRDFMV NKVPFPLPSP QIFNLDQINA LTTDTLVSDN ALKFQDLDLV PHKLKGYPVE FLIQYRKGGP NFGSTVSEKI PTDF YP

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Macromolecule #6: Acyl carrier protein 2, mitochondrial

MacromoleculeName: Acyl carrier protein 2, mitochondrial / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 14.183111 KDa
SequenceString:
MAARGAMLRY LRVNVNPTIQ NPRECVLPFS ILLRRFSEEV RGSFLDKSEV TDRVLSVVKN FQKVDPSKVT PKANFQNDLG LDSLDSVEV VMALEEEFGF EIPDNEADKI QSIDLAVDFI ASHPQAK

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Macromolecule #7: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subun...

MacromoleculeName: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5, mitochondrial
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 19.201906 KDa
SequenceString:
MFLRAIGRPL LAKVKQTTGI VGLDVVPNAR AVLIDLYSKT LKEIQAVPED EGYRKAVESF TRQRLNVCKE EEDWEMIEKR LGCGQVEEL IEEARDELTL IGKMIEWDPW GVPDDYECEV IENDAPIPKH VPQHRPGPLP EQFYKTLEGL IAESKTEIPA A TPSDPQLK E

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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: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A

MacromoleculeName: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 16.145584 KDa
SequenceString:
MTEAMIRNKP GMASVKDMPL LQDGPPPGGF APVRYARRIS NTGPSAMAMF LAVSGAFAWG MYQVGQGNKI RRALKEEKYA ARRTILPIL QAEEDERFVS EWKKYLEYEA DVMKDVPGWK VGENVYNSGR WMPPATGELR PDVW

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Macromolecule #10: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MacromoleculeName: Probable NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 18.346736 KDa
SequenceString:
MALTVAKSAL EAIREKGLGG FMRMIREEGF MRCLPDGNLL QTKIHNIGAT LVGVDKFGNK YYQKLGDTQY GRHRWVEYAS KDRYNASQV PAEWHGWLHF ITDHTGDELL SLKPKRYGLE HKENFSGEGD AYIYHSKGHT LNPGQKNWTR YQSWVPTKTQ

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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: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 12 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

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Macromolecule #13: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-b...

MacromoleculeName: S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate
type: ligand / ID: 13 / Number of copies: 1 / Formula: 8Q1
Molecular weightTheoretical: 540.651 Da
Chemical component information

ChemComp-8Q1:
S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] dodecanethioate

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Macromolecule #14: water

MacromoleculeName: water / type: ligand / ID: 14 / Number of copies: 631 / 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: 2.04 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-8bee:
Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (CI peripheral core)

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