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- PDB-7tgh: Cryo-EM structure of respiratory super-complex CI+III2 from Tetra... -

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Entry
Database: PDB / ID: 7tgh
TitleCryo-EM structure of respiratory super-complex CI+III2 from Tetrahymena thermophila
Components
  • (Acyl carrier ...) x 2
  • (Gamma-carbonic ...) x 2
  • (NADH dehydrogenase [ubiquinone] ...) x 3
  • (NADH dehydrogenase subunit ...) x 6
  • (NADH-ubiquinone oxidoreductase ...) x 7
  • (Transmembrane protein, ...) x 13
  • 2 iron, 2 sulfur cluster-binding protein
  • Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II
  • Apocytochrome b
  • Cytochrome protein c1
  • DnaJ domain protein
  • ETC complex I subunit motif protein
  • GRAM domain protein
  • Lipid-A-disaccharide synthase
  • M16 family peptidase, putative
  • NAD-dependent epimerase/dehydratase family protein
  • NADH dehydrogenase, putative
  • NDUA1
  • NDUA13
  • NDUA7
  • NDUA8
  • NDUB10
  • NDUB2
  • NDUB4
  • NDUB6
  • NDUB7
  • NDUB8
  • NDUB9
  • NDUC2
  • NDUPH2
  • NDUTT10
  • NDUTT12
  • NDUTT3
  • NDUTT4
  • NDUTT6
  • NDUTT8
  • NDUTT9
  • Peptidase M16 inactive domain protein
  • Ribosomal protein L51/S25/CI-B8 domain protein
  • Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit
  • Thioredoxin
  • Transcription factor apfi protein, putative
  • UNK1
  • UNK2
  • UNK3
  • UNK4
  • UNK5
  • UQCRB
  • Ubiquinol-cytochrome C reductase hinge protein
  • Ymf57
  • Ymf58
  • Ymf62
  • Ymf65
  • Zinc-finger protein
KeywordsMEMBRANE PROTEIN / Mitochondrial respiration / Electron transport chain / Oxidoreductase / Super-complex CI+III2
Function / homology
Function and homology information


NADH:ubiquinone reductase (H+-translocating) / lipid-A-disaccharide synthase / lipid-A-disaccharide synthase activity / quinol-cytochrome-c reductase / medium-chain fatty acid-CoA ligase activity / P450-containing electron transport chain / protein processing involved in protein targeting to mitochondrion / : / ubiquinone-6 biosynthetic process / ubiquinol-cytochrome-c reductase activity ...NADH:ubiquinone reductase (H+-translocating) / lipid-A-disaccharide synthase / lipid-A-disaccharide synthase activity / quinol-cytochrome-c reductase / medium-chain fatty acid-CoA ligase activity / P450-containing electron transport chain / protein processing involved in protein targeting to mitochondrion / : / ubiquinone-6 biosynthetic process / ubiquinol-cytochrome-c reductase activity / oxidoreductase activity, acting on NAD(P)H / NADH dehydrogenase activity / lipid A biosynthetic process / mitochondrial electron transport, ubiquinol to cytochrome c / NADH:ubiquinone reductase (H+-translocating) / chloroplast thylakoid membrane / acyl binding / ubiquinone binding / acyl carrier activity / quinone binding / electron transport coupled proton transport / : / ATP synthesis coupled electron transport / mitochondrial respiratory chain complex I assembly / fatty acid metabolic process / respiratory electron transport chain / chloroplast / : / mitochondrion organization / mitochondrial electron transport, NADH to ubiquinone / NADH dehydrogenase (ubiquinone) activity / electron transport chain / mitochondrial membrane / aerobic respiration / phospholipid binding / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / NAD binding / FMN binding / 4 iron, 4 sulfur cluster binding / response to oxidative stress / membrane => GO:0016020 / oxidoreductase activity / electron transfer activity / mitochondrial inner membrane / ribosome / heme binding / negative regulation of apoptotic process / protein-containing complex binding / protein kinase binding / mitochondrion / membrane / metal ion binding / plasma membrane / cytosol
Similarity search - Function
Glycosyl transferase, family 19 / Lipid-A-disaccharide synthetase / : / : / : / : / Dynactin subunit 5 / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Adrenodoxin ...Glycosyl transferase, family 19 / Lipid-A-disaccharide synthetase / : / : / : / : / Dynactin subunit 5 / NADH-ubiquinone oxidoreductase, 21kDa subunit, N-terminal / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Adrenodoxin / DnaJ domain / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / : / DnaJ molecular chaperone homology domain / dnaJ domain profile. / Cytochrome c1 / Cytochrome C1 family / Chaperone J-domain superfamily / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / DnaJ domain / Hexapeptide repeat / 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 / 2Fe-2S iron-sulfur cluster binding domain / : / Soluble ligand binding domain / Rieske iron-sulphur protein / SLBB domain / Bacterial transferase hexapeptide (six repeats) / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / NADH dehydrogenase ubiquinone Fe-S protein 4-like superfamily / NADH dehydrogenase ubiquinone Fe-S protein 4 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 2 / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / ETC complex I subunit conserved region / NADH ubiquinone oxidoreductase subunit NDUFA12 / NADH dehydrogenase [ubiquinone] (complex I), alpha subcomplex, subunit 6 / NADH-quinone oxidoreductase, chain G, C-terminal / : / NADH-ubiquinone oxidoreductase subunit G, C-terminal / Thioredoxin / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / Trimeric LpxA-like superfamily / 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: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 / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. / 2Fe-2S iron-sulfur cluster binding domain / NADH-quinone oxidoreductase, chain 5-like / NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / AMP-dependent synthetase/ligase / AMP-binding enzyme / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH-ubiquinone oxidoreductase-G iron-sulfur binding region / NADH:ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 3 superfamily / NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 / NADH:ubiquinone oxidoreductase, subunit 1, conserved site / Respiratory-chain NADH dehydrogenase subunit 1 signature 1. / Respiratory-chain NADH dehydrogenase subunit 1 signature 2. / NADH:ubiquinone oxidoreductase, subunit 1/F420H2 oxidoreductase subunit H / NADH dehydrogenase / NADH:ubiquinone oxidoreductase / NADH:quinone oxidoreductase/Mrp antiporter, membrane subunit / NuoE domain / Proton-conducting membrane transporter / NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding / His(Cys)3-ligated-type [4Fe-4S] domain profile. / NADH-quinone oxidoreductase subunit E-like / Thioredoxin-like [2Fe-2S] ferredoxin / NADH-quinone oxidoreductase subunit E, N-terminal
Similarity search - Domain/homology
1,2-Distearoyl-sn-glycerophosphoethanolamine / ADENOSINE-5'-DIPHOSPHATE / CARDIOLIPIN / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-NDP / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / IRON/SULFUR CLUSTER ...1,2-Distearoyl-sn-glycerophosphoethanolamine / ADENOSINE-5'-DIPHOSPHATE / CARDIOLIPIN / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-NDP / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / IRON/SULFUR CLUSTER / UBIQUINONE-10 / Chem-ZMP / Transmembrane protein, putative / NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 / NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit / Transmembrane protein, putative / Uncharacterized protein / Uncharacterized protein / Transmembrane protein / NADH dehydrogenase, putative / Transmembrane protein, putative / Gamma-carbonic anhydrase / Transmembrane protein / Transcription factor apfi protein, putative / Transmembrane protein, putative / Ribosomal protein L51/S25/CI-B8 domain protein / Transmembrane protein / Acyl carrier protein / NADH-ubiquinone oxidoreductase 1, chain, putative / NADH-ubiquinone oxidoreductase 24 kDa subunit / Transmembrane protein, putative / Transmembrane protein / Peptidase M16 inactive domain protein / Transmembrane protein, putative / Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit / Transmembrane protein / Uncharacterized protein / Transmembrane protein, putative / Uncharacterized protein / M16 family peptidase, putative / Zinc-finger protein / NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial / NAD-dependent epimerase/dehydratase family protein / Transmembrane protein, putative / Transmembrane protein / NADH dehydrogenase subunit 1 / Thioredoxin / Ubiquinol-cytochrome C reductase hinge protein / Transmembrane protein, putative / DnaJ domain protein / lipid-A-disaccharide synthase / Transmembrane protein / Transmembrane protein, putative / Transmembrane protein / Transmembrane protein, putative / 2 iron, 2 sulfur cluster-binding protein / Transmembrane protein / Acyl carrier protein / Gamma-carbonic anhydrase / Transmembrane protein, putative / Transmembrane protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / NADH-ubiquinone oxidoreductase 75 kDa subunit / Uncharacterized protein / NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial / Uncharacterized protein / ETC complex I subunit motif protein / Transmembrane protein, putative / Transmembrane protein, putative / Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II / Cytochrome protein c1 / NADH-ubiquinone oxidoreductase chain 4 / Ymf62 / NADH-ubiquinone oxidoreductase chain 1 / NADH dehydrogenase subunit 5 / Apocytochrome b / NADH dehydrogenase subunit 9 / Ymf58 / NADH-ubiquinone oxidoreductase chain 3 / Ymf65 / NADH dehydrogenase subunit 7 / NADH dehydrogenase subunit 2 / NADH dehydrogenase subunit 10 / Ymf57 / GRAM domain protein
Similarity search - Component
Biological speciesTetrahymena thermophila (eukaryote)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.6 Å
AuthorsZhou, L. / Maldonado, M. / Padavannil, A. / Guo, F. / Letts, J.A.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM137929 United States
CitationJournal: Science / Year: 2022
Title: Structures of 's respiratory chain reveal the diversity of eukaryotic core metabolism.
Authors: Long Zhou / María Maldonado / Abhilash Padavannil / Fei Guo / James A Letts /
Abstract: Respiration is a core biological energy-converting process whose last steps are carried out by a chain of multisubunit complexes in the inner mitochondrial membrane. To probe the functional and ...Respiration is a core biological energy-converting process whose last steps are carried out by a chain of multisubunit complexes in the inner mitochondrial membrane. To probe the functional and structural diversity of eukaryotic respiration, we examined the respiratory chain of the ciliate (Tt). Using cryo-electron microscopy on a mixed sample, we solved structures of a supercomplex between Tt complex I (Tt-CI) and Tt-CIII (Tt-SC I+III) and a structure of Tt-CIV. Tt-SC I+III (~2.3 megadaltons) is a curved assembly with structural and functional symmetry breaking. Tt-CIV is a ~2.7-megadalton dimer with more than 50 subunits per protomer, including mitochondrial carriers and a TIM8-TIM13-like domain. Our structural and functional study of the respiratory chain reveals divergence in key components of eukaryotic respiration, thereby expanding our understanding of core metabolism.
History
DepositionJan 7, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 6, 2022Provider: repository / Type: Initial release
Revision 1.1Jul 20, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
1: NADH-ubiquinone oxidoreductase chain 1
1B: NADH dehydrogenase subunit 1
2: Ymf65
2B: NADH dehydrogenase subunit 2
3: NADH-ubiquinone oxidoreductase chain 3
3A: M16 family peptidase, putative
3B: Peptidase M16 inactive domain protein
3C: Apocytochrome b
3D: Cytochrome protein c1
3E: Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit
3F: Ubiquinol-cytochrome C reductase hinge protein
3G: UQCRB
3H: Transmembrane protein, putative
3I: Transmembrane protein, putative
3J: Transmembrane protein, putative
3M: UNK1
3a: M16 family peptidase, putative
3b: Peptidase M16 inactive domain protein
3c: Apocytochrome b
3d: Cytochrome protein c1
3e: Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit
3f: Ubiquinol-cytochrome C reductase hinge protein
3g: UQCRB
3h: Transmembrane protein, putative
3i: Transmembrane protein, putative
3j: Transmembrane protein, putative
3l: UNK2
3m: UNK3
4: NADH-ubiquinone oxidoreductase chain 4
4L: Ymf58
5: NADH dehydrogenase subunit 5
5B: Ymf57
6: Ymf62
A2: Ribosomal protein L51/S25/CI-B8 domain protein
A5: ETC complex I subunit motif protein
A6: NADH dehydrogenase, putative
A7: NDUA7
A9: NAD-dependent epimerase/dehydratase family protein
AB: Acyl carrier protein
AC: Acyl carrier protein
AL: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
AM: NDUA13
B7: NDUB7
B8: NDUB8
BL: NDUB10
C: UNK4
C1: Gamma-carbonic anhydrase
C2: Gamma-carbonic anhydrase
C3: Transcription factor apfi protein, putative
TD: Transmembrane protein, putative
J1: DnaJ domain protein
FX: 2 iron, 2 sulfur cluster-binding protein
T2: Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II
T1: Lipid-A-disaccharide synthase
A1: NDUA1
X1: NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit
T6: NDUTT6
T5: Transmembrane protein, putative
R: UNK5
S1: NADH-ubiquinone oxidoreductase 75 kDa subunit
S2: NADH dehydrogenase subunit 7
S3: NADH dehydrogenase subunit 9
S4: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial
S6: Zinc-finger protein
S7: NADH dehydrogenase subunit 10
S8: NADH-ubiquinone oxidoreductase 1, chain, putative
B9: NDUB9
TX: Thioredoxin
A8: NDUA8
TB: Transmembrane protein, putative
V1: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial
V2: NADH-ubiquinone oxidoreductase 24 kDa subunit
B6: NDUB6
BM: Transmembrane protein, putative
C4: NDUC2
AN: Transmembrane protein, putative
B4: NDUB4
T4: NDUTT4
T8: NDUTT8
B2: NDUB2
T3: NDUTT3
P1: Transmembrane protein, putative
B3: Transmembrane protein, putative
TA: NDUTT10
S5: GRAM domain protein
TC: NDUTT12
P2: NDUPH2
A3: Transmembrane protein, putative
T9: NDUTT9
TE: Transmembrane protein, putative
T7: Transmembrane protein, putative
hetero molecules


Theoretical massNumber of molelcules
Total (without water)2,416,172195
Polymers2,324,21391
Non-polymers91,959104
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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NADH-ubiquinone oxidoreductase ... , 7 types, 7 molecules 134X1S1S8V2

#1: Protein NADH-ubiquinone oxidoreductase chain 1


Mass: 32636.770 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
References: UniProt: Q950Y3, NADH:ubiquinone reductase (H+-translocating)
#5: Protein NADH-ubiquinone oxidoreductase chain 3


Mass: 14416.898 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
References: UniProt: Q950Z7, NADH:ubiquinone reductase (H+-translocating)
#19: Protein NADH-ubiquinone oxidoreductase chain 4


Mass: 58690.043 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
References: UniProt: Q950X9, NADH:ubiquinone reductase (H+-translocating)
#46: Protein NADH-ubiquinone oxidoreductase complex I, 21 kDa subunit


Mass: 17381.809 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7LT42
#50: Protein NADH-ubiquinone oxidoreductase 75 kDa subunit


Mass: 80580.789 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q23KA9
#56: Protein NADH-ubiquinone oxidoreductase 1, chain, putative


Mass: 28053.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MDW5
#62: Protein NADH-ubiquinone oxidoreductase 24 kDa subunit


Mass: 31216.697 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MEP0

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NADH dehydrogenase subunit ... , 6 types, 6 molecules 1B2B5S2S3S7

#2: Protein NADH dehydrogenase subunit 1


Mass: 7238.754 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q09FB0
#4: Protein NADH dehydrogenase subunit 2


Mass: 20899.889 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
References: UniProt: Q951B2, NADH:ubiquinone reductase (H+-translocating)
#21: Protein NADH dehydrogenase subunit 5


Mass: 88179.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
References: UniProt: Q950Z0, NADH:ubiquinone reductase (H+-translocating)
#51: Protein NADH dehydrogenase subunit 7


Mass: 51227.477 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
References: UniProt: Q951B1, NADH:ubiquinone reductase (H+-translocating)
#52: Protein NADH dehydrogenase subunit 9


Mass: 23803.268 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
References: UniProt: Q950Z4, NADH:ubiquinone reductase (H+-translocating)
#55: Protein NADH dehydrogenase subunit 10


Mass: 18324.260 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
References: UniProt: Q951B4, NADH:ubiquinone reductase (H+-translocating)

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Protein , 45 types, 52 molecules 23A3a3B3b3C3c3D3d3E3e3F3f3G3g4L5B6A2A5A6A7A9AMB7B8BLCC3J1...

#3: Protein Ymf65


Mass: 43104.082 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q951A3
#6: Protein M16 family peptidase, putative


Mass: 53030.543 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MJ25
#7: Protein Peptidase M16 inactive domain protein


Mass: 58023.914 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MGU2
#8: Protein Apocytochrome b


Mass: 50635.547 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q950Z1, quinol-cytochrome-c reductase
#9: Protein Cytochrome protein c1


Mass: 37616.629 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q24IM5
#10: Protein Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit


Mass: 30696.961 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MIC7
#11: Protein Ubiquinol-cytochrome C reductase hinge protein


Mass: 10249.956 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22AX2
#12: Protein UQCRB


Mass: 39193.523 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q23F81
#20: Protein Ymf58


Mass: 13509.949 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q950Z5
#22: Protein Ymf57


Mass: 12473.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q951C2
#23: Protein Ymf62


Mass: 30448.471 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q950Y2
#24: Protein Ribosomal protein L51/S25/CI-B8 domain protein


Mass: 12157.782 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MA77
#25: Protein ETC complex I subunit motif protein


Mass: 24277.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q23ND5
#26: Protein NADH dehydrogenase, putative


Mass: 20167.854 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7M2Y3
#27: Protein NDUA7


Mass: 33201.797 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MIJ7
#28: Protein NAD-dependent epimerase/dehydratase family protein


Mass: 41375.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MLH2
#32: Protein NDUA13


Mass: 21045.617 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7M2U4
#33: Protein NDUB7


Mass: 13747.362 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MIM0
#34: Protein NDUB8


Mass: 24150.469 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7M855
#35: Protein NDUB10


Mass: 22167.137 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q23KG0
#36: Protein UNK4


Mass: 17804.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
#39: Protein Transcription factor apfi protein, putative


Mass: 39793.414 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7M8Q7
#41: Protein DnaJ domain protein


Mass: 36878.367 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22DR7
#42: Protein 2 iron, 2 sulfur cluster-binding protein


Mass: 19564.221 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22W11
#43: Protein Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II


Mass: 36709.441 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q24HK5
#44: Protein Lipid-A-disaccharide synthase


Mass: 59307.289 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22E24, lipid-A-disaccharide synthase
#45: Protein NDUA1


Mass: 11451.183 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MI60
#47: Protein NDUTT6


Mass: 17078.342 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7M1N8
#49: Protein UNK5


Mass: 13356.364 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
#54: Protein Zinc-finger protein


Mass: 15141.296 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MK02
#57: Protein NDUB9


Mass: 22698.301 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q233X7
#58: Protein Thioredoxin


Mass: 19540.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22AI5
#59: Protein NDUA8


Mass: 28412.805 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MMF4
#63: Protein NDUB6


Mass: 15444.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q231G0
#65: Protein NDUC2


Mass: 12103.036 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22W63
#67: Protein NDUB4


Mass: 12577.971 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
#68: Protein NDUTT4


Mass: 24823.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MIE0
#69: Protein NDUTT8


Mass: 15785.234 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22SC4
#70: Protein NDUB2


Mass: 14410.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MG29
#71: Protein NDUTT3


Mass: 35409.246 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7LUQ4
#74: Protein NDUTT10


Mass: 12123.922 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MAF0
#75: Protein GRAM domain protein


Mass: 10920.431 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: W7X4R4
#76: Protein NDUTT12


Mass: 11283.534 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22E95
#77: Protein NDUPH2


Mass: 22446.637 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q23KE0
#79: Protein NDUTT9


Mass: 15576.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q23B10

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Transmembrane protein, ... , 13 types, 16 molecules 3H3h3I3i3J3jTDT5TBBMANP1B3A3TET7

#13: Protein Transmembrane protein, putative


Mass: 15677.771 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7M484
#14: Protein Transmembrane protein, putative


Mass: 14262.554 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MM45
#15: Protein Transmembrane protein, putative


Mass: 7455.741 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MFL6
#40: Protein Transmembrane protein, putative


Mass: 8787.116 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22DC2
#48: Protein Transmembrane protein, putative


Mass: 23971.033 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7LT77
#60: Protein Transmembrane protein, putative


Mass: 13340.979 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22T55
#64: Protein Transmembrane protein, putative


Mass: 24419.150 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22Z32
#66: Protein Transmembrane protein, putative


Mass: 26545.146 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q24F24
#72: Protein Transmembrane protein, putative


Mass: 29389.660 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q24C39
#73: Protein Transmembrane protein, putative


Mass: 9942.366 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: A4VD20
#78: Protein Transmembrane protein, putative


Mass: 15831.701 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7M9B3
#80: Protein Transmembrane protein, putative


Mass: 8445.937 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MIK1
#81: Protein Transmembrane protein, putative


Mass: 16909.242 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22HE4

-
Protein/peptide , 3 types, 3 molecules 3M3l3m

#16: Protein/peptide UNK1


Mass: 2181.579 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
#17: Protein/peptide UNK2


Mass: 1781.919 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
#18: Protein/peptide UNK3


Mass: 1725.046 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255

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Acyl carrier ... , 2 types, 2 molecules ABAC

#29: Protein Acyl carrier protein


Mass: 16249.438 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22XT6
#30: Protein Acyl carrier protein


Mass: 15428.433 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MD12

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NADH dehydrogenase [ubiquinone] ... , 3 types, 3 molecules ALS4V1

#31: Protein NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12


Mass: 22890.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: A4VDQ6
#53: Protein NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial


Mass: 21642.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7MK61
#61: Protein NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial


Mass: 52313.699 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255
References: UniProt: Q23KE4, NADH:ubiquinone reductase (H+-translocating)

-
Gamma-carbonic ... , 2 types, 2 molecules C1C2

#37: Protein Gamma-carbonic anhydrase


Mass: 28216.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: Q22XU5
#38: Protein Gamma-carbonic anhydrase


Mass: 25395.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Tetrahymena thermophila (eukaryote) / Strain: SB255 / References: UniProt: I7M6S0

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Non-polymers , 13 types, 104 molecules

#82: Chemical...
ChemComp-CDL / CARDIOLIPIN / DIPHOSPHATIDYL GLYCEROL / BIS-(1,2-DIACYL-SN-GLYCERO-3-PHOSPHO)-1',3'-SN-GLYCEROL


Mass: 1464.043 Da / Num. of mol.: 29 / Source method: obtained synthetically / Formula: C81H156O17P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
#83: Chemical...
ChemComp-PC1 / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / 3-SN-PHOSPHATIDYLCHOLINE


Mass: 790.145 Da / Num. of mol.: 32 / Source method: obtained synthetically / Formula: C44H88NO8P / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
#84: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#85: Chemical ChemComp-U10 / UBIQUINONE-10 / Coenzyme Q10


Mass: 863.343 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C59H90O4 / Feature type: SUBJECT OF INVESTIGATION
#86: Chemical ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H34FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#87: Chemical
ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe2S2 / Feature type: SUBJECT OF INVESTIGATION
#88: Chemical
ChemComp-3PE / 1,2-Distearoyl-sn-glycerophosphoethanolamine / 3-SN-PHOSPHATIDYLETHANOLAMINE / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE


Mass: 748.065 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: C41H82NO8P / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
#89: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#90: Chemical ChemComp-NDP / NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE


Mass: 745.421 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H30N7O17P3 / Feature type: SUBJECT OF INVESTIGATION
#91: Chemical ChemComp-ZMP / S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate


Mass: 568.704 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C25H49N2O8PS / Feature type: SUBJECT OF INVESTIGATION
#92: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM
#93: Chemical
ChemComp-SF4 / IRON/SULFUR CLUSTER


Mass: 351.640 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Fe4S4 / Feature type: SUBJECT OF INVESTIGATION
#94: Chemical ChemComp-FMN / FLAVIN MONONUCLEOTIDE / RIBOFLAVIN MONOPHOSPHATE


Mass: 456.344 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C17H21N4O9P / Feature type: SUBJECT OF INVESTIGATION

-
Details

Has ligand of interestY

-
Experimental details

-
Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

-
Sample preparation

ComponentName: Mitochondrial Super-complex I+III2 of Tetrahymena thermophila
Type: COMPLEX / Entity ID: #1-#81 / Source: NATURAL
Molecular weightValue: 2.3 MDa / Experimental value: NO
Source (natural)Organism: Tetrahymena thermophila (eukaryote) / Strain: SB255
Buffer solutionpH: 7.4
Details: Solution were made fresh from concentrated stocks, filtered and de-gassed before equilibration onto Superose6 column
Buffer component
IDConc.NameFormulaBuffer-ID
120 mM2-Amino-2-(hydroxymethyl)propane-1,3-diol1
250 mMsodium chlorideNaCl1
35 mMmagnesium chlorideMgCl21
40.002 g/100 mlPhenylmethanesulfonyl fluoride1
SpecimenConc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: 30 mA / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K
Details: incubation time before blotting: 60s, blot time: 9s, blot force: 25, offset: -2, incubation after blotting: 0s

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Calibrated magnification: 58616 X / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 5.9 sec. / Electron dose: 66.69 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 7895

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Processing

Software
NameVersionClassification
phenix.real_space_refine1.19.2_4158refinement
PHENIX1.19.2_4158refinement
EM software
IDNameVersionCategory
2SerialEMimage acquisition
4CTFFIND4.1CTF correction
7UCSF Chimeramodel fitting
8Cootmodel fitting
10cryoSPARC3.2.0initial Euler assignment
11cryoSPARC3.2.0final Euler assignment
12cryoSPARC3.2.0classification
13cryoSPARC3.2.03D reconstruction
14PHENIX1.19.2model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 1144671
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 203834 / Algorithm: FOURIER SPACE / Num. of class averages: 1 / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 49.81 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0027157251
ELECTRON MICROSCOPYf_angle_d0.5165212535
ELECTRON MICROSCOPYf_chiral_restr0.04622399
ELECTRON MICROSCOPYf_plane_restr0.003726830
ELECTRON MICROSCOPYf_dihedral_angle_d7.910323587

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