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- EMDB-42228: High resolution in-situ structure of complex III in respiratory s... -

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Entry
Database: EMDB / ID: EMD-42228
TitleHigh resolution in-situ structure of complex III in respiratory supercomplex (composite)
Map data
Sample
  • Complex: In-situ cryo-EM structure of respiratory supercomplex by directly imaging mitochondria
    • Protein or peptide: x 7 types
  • Protein or peptide: x 3 types
  • Ligand: x 7 types
Keywordsin-situ cryo-EM structure / mammalian / mitochondria / respiratory supercomplex / proton pumping / membrane protein / electron transport
Function / homology
Function and homology information


respiratory chain complex III / Respiratory electron transport / mitochondrial respiratory chain complex IV / Mitochondrial protein degradation / mitochondrial respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding ...respiratory chain complex III / Respiratory electron transport / mitochondrial respiratory chain complex IV / Mitochondrial protein degradation / mitochondrial respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / mitochondrial inner membrane / membrane => GO:0016020 / electron transfer activity / heme binding / mitochondrion / proteolysis / nucleoplasm / metal ion binding / plasma membrane
Similarity search - Function
Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Globular protein, non-globular alpha/beta subunit / Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily ...Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Globular protein, non-globular alpha/beta subunit / Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome b / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / Cytochrome c1 / Cytochrome C1 family / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily
Similarity search - Domain/homology
Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome c1, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial / Cytochrome b-c1 complex subunit 8 / Complex III subunit 9 / Cytochrome b-c1 complex subunit 6 / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit 10 / Cytochrome b
Similarity search - Component
Biological speciesSus scrofa (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.1 Å
AuthorsZheng W / Zhu J / Zhang K
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R35GM142959 United States
CitationJournal: Nature / Year: 2024
Title: High-resolution in situ structures of mammalian respiratory supercomplexes.
Authors: Wan Zheng / Pengxin Chai / Jiapeng Zhu / Kai Zhang /
Abstract: Mitochondria play a pivotal part in ATP energy production through oxidative phosphorylation, which occurs within the inner membrane through a series of respiratory complexes. Despite extensive in ...Mitochondria play a pivotal part in ATP energy production through oxidative phosphorylation, which occurs within the inner membrane through a series of respiratory complexes. Despite extensive in vitro structural studies, determining the atomic details of their molecular mechanisms in physiological states remains a major challenge, primarily because of loss of the native environment during purification. Here we directly image porcine mitochondria using an in situ cryo-electron microscopy approach. This enables us to determine the structures of various high-order assemblies of respiratory supercomplexes in their native states. We identify four main supercomplex organizations: IIIIIV, IIIIIV, IIIIIV and IIIIIV, which potentially expand into higher-order arrays on the inner membranes. These diverse supercomplexes are largely formed by 'protein-lipids-protein' interactions, which in turn have a substantial impact on the local geometry of the surrounding membranes. Our in situ structures also capture numerous reactive intermediates within these respiratory supercomplexes, shedding light on the dynamic processes of the ubiquinone/ubiquinol exchange mechanism in complex I and the Q-cycle in complex III. Structural comparison of supercomplexes from mitochondria treated under different conditions indicates a possible correlation between conformational states of complexes I and III, probably in response to environmental changes. By preserving the native membrane environment, our approach enables structural studies of mitochondrial respiratory supercomplexes in reaction at high resolution across multiple scales, from atomic-level details to the broader subcellular context.
History
DepositionOct 5, 2023-
Header (metadata) releaseJun 19, 2024-
Map releaseJun 19, 2024-
UpdateJun 19, 2024-
Current statusJun 19, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_42228.png

Downloads & links

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Map

FileDownload / File: emd_42228.map.gz / Format: CCP4 / Size: 518 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.42 Å/pix.
x 514 pix.
= 213.824 Å		0.42 Å/pix.
x 514 pix.
= 213.824 Å		0.42 Å/pix.
x 514 pix.
= 213.824 Å

Surface

Projections

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.416 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-0.000000005336493 - 1.6264501
Average (Standard dev.)0.010371922 (±0.048777435)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-1-1-1
Dimensions514514514
Spacing514514514
CellA=B=C: 213.824 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_42228_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_42228_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : In-situ cryo-EM structure of respiratory supercomplex by directly...

EntireName: In-situ cryo-EM structure of respiratory supercomplex by directly imaging mitochondria
Components
  • Complex: In-situ cryo-EM structure of respiratory supercomplex by directly imaging mitochondria
    • Protein or peptide: Cytochrome b-c1 complex subunit 1, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 2, mitochondrial
    • Protein or peptide: Cytochrome b-c1 complex subunit 7
    • Protein or peptide: Cytochrome b-c1 complex subunit 8
    • Protein or peptide: Cytochrome b-c1 complex subunit 6, mitochondrial
    • Protein or peptide: Ubiquinol-cytochrome c reductase complex 7.2 kDa protein
    • Protein or peptide: Cytochrome b-c1 complex subunit 10
  • Protein or peptide: Cytochrome b
  • Protein or peptide: Cytochrome c1, heme protein, mitochondrial
  • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
  • Ligand: CARDIOLIPIN
  • Ligand: 1,2-Distearoyl-sn-glycerophosphoethanolamine
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: HEME C
  • Ligand: FE2/S2 (INORGANIC) CLUSTER
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
  • Ligand: water

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Supramolecule #1: In-situ cryo-EM structure of respiratory supercomplex by directly...

SupramoleculeName: In-situ cryo-EM structure of respiratory supercomplex by directly imaging mitochondria
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2, #6-#10
Source (natural)Organism: Sus scrofa (pig)

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

MacromoleculeName: Cytochrome b-c1 complex subunit 1, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 52.75632 KDa
SequenceString: MAASAVCRVA GTGSRVLLRT CRSPALLRSP ALRGTATYAQ ALQSVPETQV SQLDNGLRVA SEQSSQPTCT VGVWIDAGSR YENEKNNGA GYFVEHLAFK GTKNRPGSAL EKEVESMGAH LNAYSTREHT AYYIKALSKD LPKAVELLAD IVQNCSLEDS Q IEKERDVI ...String:
MAASAVCRVA GTGSRVLLRT CRSPALLRSP ALRGTATYAQ ALQSVPETQV SQLDNGLRVA SEQSSQPTCT VGVWIDAGSR YENEKNNGA GYFVEHLAFK GTKNRPGSAL EKEVESMGAH LNAYSTREHT AYYIKALSKD LPKAVELLAD IVQNCSLEDS Q IEKERDVI LQELQENDSS MRDVVFDYLH ATAFQGTPLA QSVEGPSENV RKLSRADLTE YVSQHYKAPR MVLAAAGGVE HR QLLDLAQ KHFSSLSGTY VEDAVPAFTP CRFTGSEIRH RDDALPLAHV AIAVEGPGWA NPDNVPLQVA NAIIGHYDST YGG GTHMSS TLASVAATRK LCQSFQTFNI CYAETGLLGA HFVCDNMSID DMMFFLQGQW MRLCTSATES EVVRGKNILR NALV SHLDG TTPVCEDIGR SLLTYGRRIP LAEWESRIAE VDASVVREVC SKYFYDQCPA VAGLGPIEQL PDYNRIRSGM FWLRF

UniProtKB: Cytochrome b-c1 complex subunit 1, mitochondrial

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

MacromoleculeName: Cytochrome b-c1 complex subunit 2, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 48.262434 KDa
SequenceString: MKLITRAGSF SRFYSLKVAP KALASAAPAG VPLQPQDLEF TRLPNGLVIA SLENYAPASR IGLFIKAGSR YEDSNNLGTS HLLRLASSL TTKGASSFKI TRGIEAVGGK LSVTSTRESM AYTVECLRDD IEILMEFLLN VTAAPEFRRW EVAALQSQLR I DKAVAFQN ...String:
MKLITRAGSF SRFYSLKVAP KALASAAPAG VPLQPQDLEF TRLPNGLVIA SLENYAPASR IGLFIKAGSR YEDSNNLGTS HLLRLASSL TTKGASSFKI TRGIEAVGGK LSVTSTRESM AYTVECLRDD IEILMEFLLN VTAAPEFRRW EVAALQSQLR I DKAVAFQN PQAQVLENLH AAAYRNALAN SLYCPDYRIG KVTPDQLHYY VQNHFTSARM ALIGLGVSHP VLKQVAERFL NM RGGLGLS GAKAKYRGGE IRDQNGDSLV HAALVAESAA TGSAEANAFS VLQHVLGAGP HVKRGSNATS SLYQAVAKGV HQP FDVSAF NASYSDSGLF GIYTISQAAS AGDVIKSAYD QVKTIAQGNL SNTDVQAAKN KLKAGYLMSV ESSEGFLDEV GSQA LVAGS YVQPSTVLQQ IDSVADADVI NAAKKFVSGR KSMAASGNLG HTPFVDEL

UniProtKB: Cytochrome b-c1 complex subunit 2, mitochondrial

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Macromolecule #3: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 42.840715 KDa
SequenceString: MTNIRKSHPL MKIINNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWVIR YLHANGASM FFICLFIHVG RGLYYGSYMF LETWNIGVVL LFTVMATAFM GYVLPWGQMS FWGATVITNL LSAIPYIGTD L VEWIWGGF ...String:
MTNIRKSHPL MKIINNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWVIR YLHANGASM FFICLFIHVG RGLYYGSYMF LETWNIGVVL LFTVMATAFM GYVLPWGQMS FWGATVITNL LSAIPYIGTD L VEWIWGGF SVDKATLTRF FAFHFILPFI ITALAAVHLL FLHETGSNNP TGISSDMDKI PFHPYYTIKD ILGALFMMLI LL ILVLFSP DLLGDPDNYT PANPLNTPPH IKPEWYFLFA YAILRSIPNK LGGVLALVAS ILILILMPML HTSKQRSMMF RPL SQCLFW MLVADLITLT WIGGQPVEHP FIIIGQLASI LYFLIILVLM PITSIIENNL LKW

UniProtKB: Cytochrome b

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Macromolecule #4: Cytochrome c1, heme protein, mitochondrial

MacromoleculeName: Cytochrome c1, heme protein, mitochondrial / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 35.35975 KDa
SequenceString: MSAAAAASLR GAVLGPRGAG LPGARARGLL CGPRPGQLPL RTPQALSLSS KSGLSRGRKV ILSALGMLAA GGAGLAVALH SAVSATDLE LHAPSYPWSH RGLLSSLDHT SIRRGFQVYK QVCSSCHSMD YVAYRHLVGV CYTEEEAKAL AEEVEVQDGP N EDGEMFMR ...String:
MSAAAAASLR GAVLGPRGAG LPGARARGLL CGPRPGQLPL RTPQALSLSS KSGLSRGRKV ILSALGMLAA GGAGLAVALH SAVSATDLE LHAPSYPWSH RGLLSSLDHT SIRRGFQVYK QVCSSCHSMD YVAYRHLVGV CYTEEEAKAL AEEVEVQDGP N EDGEMFMR PGKLSDYFPK PYPNPEAARA ANNGALPPDL SYIVRARHGG EDYVFSLLTG YCEPPTGVSL REGLYFNPYF PG QAIAMAP PIYNEVLEFD DGTPATMSQV AKDVCTFLRW ASEPEHDHRK RMGLKMLMMM GLLLPLVYAM KRHKWSVLKS RKL AYRPP

UniProtKB: Cytochrome c1, heme protein, mitochondrial

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

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske, mitochondrial / type: protein_or_peptide / ID: 5 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 29.4926 KDa
SequenceString: MLSVASRSGP FAPVLSATSR GVAGALRPLV QAALPATSES PVLDAKRSFL CRESLSGQAA GRPLVASVGL NVPASVRYSH TDIRVPDFS DYRRAEVLDS TKSSKESSDA RKGFSYLITA TTTVGVAYAA KNAVSQFVSS MSASADVLAM SKIEIKLSDI P EGKNMAFK ...String:
MLSVASRSGP FAPVLSATSR GVAGALRPLV QAALPATSES PVLDAKRSFL CRESLSGQAA GRPLVASVGL NVPASVRYSH TDIRVPDFS DYRRAEVLDS TKSSKESSDA RKGFSYLITA TTTVGVAYAA KNAVSQFVSS MSASADVLAM SKIEIKLSDI P EGKNMAFK WRGKPLFVRH RTKKEIDQEA AVEVSQLRDP QHDLERVKKP EWVILIGVCT HLGCVPIANA GDFGGYYCPC HG SHYDASG RIRKGPAPLN LEVPTYEFTS DDLVIVG

UniProtKB: Cytochrome b-c1 complex subunit Rieske, mitochondrial

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Macromolecule #6: Cytochrome b-c1 complex subunit 7

MacromoleculeName: Cytochrome b-c1 complex subunit 7 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 13.587549 KDa
SequenceString:
MASRPAVAAS SKWLEGIRKW YYNAAGFNKL GLMRDDTIYE DDDVKEAIRR LPENLYNDRV FRIKRALDLT MRQQILPKEQ WTKYEEDKF YLEPYLKEVI RERKEREEWA KK

UniProtKB: Cytochrome b-c1 complex subunit 7

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Macromolecule #7: Cytochrome b-c1 complex subunit 8

MacromoleculeName: Cytochrome b-c1 complex subunit 8 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 9.784339 KDa
SequenceString:
MGREFGHLTR MRHVITYSLS PFEQRAFPHY FTKGIPNVLR RTRACILRVA PPFVVFYLVY TWGTQEFEKS KRKNPAAYEN DK

UniProtKB: Cytochrome b-c1 complex subunit 8

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Macromolecule #8: Cytochrome b-c1 complex subunit 6, mitochondrial

MacromoleculeName: Cytochrome b-c1 complex subunit 6, mitochondrial / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 10.685803 KDa
SequenceString:
MGLEDEQRML TGSGDPKEEE EEEEELVDPL TTVREQCEQI EKCIKARERL ELCDQRVSSR SQTEEDCTEE LFDFLHARDH CVAHKLFNS LK

UniProtKB: Cytochrome b-c1 complex subunit 6

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Macromolecule #9: Ubiquinol-cytochrome c reductase complex 7.2 kDa protein

MacromoleculeName: Ubiquinol-cytochrome c reductase complex 7.2 kDa protein
type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 7.41253 KDa
SequenceString:
MAAPTLTARL YSLLFRRTST FALTIAVGAL FFERAFDQGA DAIYEHINQG KLWKHIKHKY ENKE

UniProtKB: Complex III subunit 9

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Macromolecule #10: Cytochrome b-c1 complex subunit 10

MacromoleculeName: Cytochrome b-c1 complex subunit 10 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 6.560654 KDa
SequenceString:
MLSRFLGPRY RELARNWIPT ASMWGAVGAV GLVWATDWRL ILDWVPYING KFKKED

UniProtKB: Cytochrome b-c1 complex subunit 10

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Macromolecule #11: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 11 / Number of copies: 6 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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Macromolecule #12: 1,2-Distearoyl-sn-glycerophosphoethanolamine

MacromoleculeName: 1,2-Distearoyl-sn-glycerophosphoethanolamine / type: ligand / ID: 12 / Number of copies: 11 / Formula: 3PE
Molecular weightTheoretical: 748.065 Da
Chemical component information

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

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Macromolecule #13: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 13 / Number of copies: 4 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

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Macromolecule #14: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 14 / Number of copies: 2 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C / Heme C

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Macromolecule #15: FE2/S2 (INORGANIC) CLUSTER

MacromoleculeName: FE2/S2 (INORGANIC) CLUSTER / type: ligand / ID: 15 / 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 #16: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 16 / Number of copies: 3 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM / Phosphatidylcholine

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Macromolecule #17: water

MacromoleculeName: water / type: ligand / ID: 17 / Number of copies: 1938 / 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

BufferpH: 7
VitrificationCryogen name: ETHANE

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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 / Cs: 2.7 mm / Nominal defocus max: 3.2 µm / Nominal defocus min: 1.0 µm
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 300000

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