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- EMDB-50204: Structure of the Chlamydomonas reinhardtii respiratory complex II... -

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Basic information

Entry
Database: EMDB / ID: EMD-50204
TitleStructure of the Chlamydomonas reinhardtii respiratory complex III from respiratory supercomplex
Map data
Sample
  • Complex: Chlamydomonas reinhardtii respirasome
    • Protein or peptide: x 10 types
  • Ligand: x 8 types
KeywordsMitochondria / respiratory complex / respiration / alga / MEMBRANE PROTEIN
Function / homology
Function and homology information


quinol-cytochrome-c reductase / respiratory chain complex III / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / metallopeptidase activity / electron transfer activity / mitochondrial inner membrane ...quinol-cytochrome-c reductase / respiratory chain complex III / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / metallopeptidase activity / electron transfer activity / mitochondrial inner membrane / oxidoreductase activity / heme binding / mitochondrion / metal ion binding
Similarity search - Function
Cytochrome b-c1 complex subunit 8, plants / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Ubiquinol-cytochrome C reductase hinge domain ...Cytochrome b-c1 complex subunit 8, plants / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex, subunit 6 / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 8 superfamily / 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 b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome c1, transmembrane anchor, C-terminal / : / Cytochrome b / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / : / Cytochrome c1 / Cytochrome C1 family / : / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulphur 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 / Uncharacterized protein / Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10 / Uncharacterized protein / Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8 / Cytochrome b-c1 complex subunit 6 / Complex III subunit 9 / Cytochrome b / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome c1
Similarity search - Component
Biological speciesChlamydomonas reinhardtii (plant)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.39 Å
AuthorsWaltz F / Righetto R / Kotecha A / Engel BD
Funding support Germany, Switzerland, 2 items
OrganizationGrant numberCountry
Alexander von Humboldt Foundation Germany
Swiss National Science Foundation210561 Switzerland
CitationJournal: Science / Year: 2025
Title: In-cell architecture of the mitochondrial respiratory chain.
Authors: Florent Waltz / Ricardo D Righetto / Lorenz Lamm / Thalia Salinas-Giegé / Ron Kelley / Xianjun Zhang / Martin Obr / Sagar Khavnekar / Abhay Kotecha / Benjamin D Engel /
Abstract: Mitochondria regenerate adenosine triphosphate (ATP) through oxidative phosphorylation. This process is carried out by five membrane-bound complexes collectively known as the respiratory chain, ...Mitochondria regenerate adenosine triphosphate (ATP) through oxidative phosphorylation. This process is carried out by five membrane-bound complexes collectively known as the respiratory chain, working in concert to transfer electrons and pump protons. The precise organization of these complexes in native cells is debated. We used in situ cryo-electron tomography to visualize the native structures and organization of several major mitochondrial complexes in cells. ATP synthases and respiratory complexes segregate into curved and flat crista membrane domains, respectively. Respiratory complexes I, III, and IV assemble into a respirasome supercomplex, from which we determined a native 5-angstrom (Å) resolution structure showing binding of electron carrier cytochrome . Combined with single-particle cryo-electron microscopy at 2.4-Å resolution, we model how the respiratory complexes organize inside native mitochondria.
History
DepositionApr 30, 2024-
Header (metadata) releaseMar 12, 2025-
Map releaseMar 12, 2025-
UpdateApr 2, 2025-
Current statusApr 2, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_50204.png

Downloads & links

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Map

FileDownload / File: emd_50204.map.gz / Format: CCP4 / Size: 775.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1 Å/pix.
x 588 pix.
= 589.6 Å		1 Å/pix.
x 588 pix.
= 589.6 Å		1 Å/pix.
x 588 pix.
= 589.6 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.00272 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.145
Minimum - Maximum-0.5338155 - 1.1168878
Average (Standard dev.)-0.000021564105 (±0.02506046)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions588588588
Spacing588588588
CellA=B=C: 589.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_50204_msk_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_50204_half_map_1.map
Projections & Slices
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Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: #1

Fileemd_50204_half_map_2.map
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Sample components

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Entire : Chlamydomonas reinhardtii respirasome

EntireName: Chlamydomonas reinhardtii respirasome
Components
  • Complex: Chlamydomonas reinhardtii respirasome
    • Protein or peptide: Cytochrome b
    • Protein or peptide: Cytochrome b-c1 complex subunit Rieske, mitochondrial
    • Protein or peptide: Cytochrome c1
    • Protein or peptide: Complex III subunit 9
    • Protein or peptide: Cytochrome b-c1 complex subunit 6
    • Protein or peptide: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8
    • Protein or peptide: MPP-Beta
    • Protein or peptide: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10
    • Protein or peptide: Alpha-MPP
    • Protein or peptide: Cytochrome b-c1 complex subunit 7
  • Ligand: 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE
  • Ligand: HEME C
  • Ligand: CARDIOLIPIN
  • Ligand: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE
  • Ligand: PHOSPHATIDYLETHANOLAMINE
  • Ligand: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE
  • Ligand: ZINC ION
  • Ligand: water

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Supramolecule #1: Chlamydomonas reinhardtii respirasome

SupramoleculeName: Chlamydomonas reinhardtii respirasome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#10
Source (natural)Organism: Chlamydomonas reinhardtii (plant)

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Macromolecule #1: Cytochrome b

MacromoleculeName: Cytochrome b / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 42.356465 KDa
SequenceString: MRMHNKIQLL SVLNTHLVAY PTPMNLNYSW NGGSLAGMML ASQMLTGILL AMHYVGHVDY AFASVQHLMT DVPSGMILRY AHANGASLF FIVVYLHVLR GMYYGSGAQP REIVWISGVV ILLVMIITAF IGYVLPWGQM SFWGATVITS LATAIPVVGK H IMYWLWGG ...String:
MRMHNKIQLL SVLNTHLVAY PTPMNLNYSW NGGSLAGMML ASQMLTGILL AMHYVGHVDY AFASVQHLMT DVPSGMILRY AHANGASLF FIVVYLHVLR GMYYGSGAQP REIVWISGVV ILLVMIITAF IGYVLPWGQM SFWGATVITS LATAIPVVGK H IMYWLWGG FSVDNPTLNR FYSFHYTLPF ILAGLSVFHI AALHQYGSTN PLGVNSQSSL ISFGSYFGAK DLVGALFLAL VF SILVFFY PDLLGHPDNL IPANPYSTPQ HIVPEWYFLW VYAILRSIPN KAMGVLAIGL VFASLFAMPF IGLGGGKFRI ITE WLYWTF LADVLLLTWL GGNEITPITS FVGQCCTAYL FFYLLVCQPL VGYLETQFAH GTQTN

UniProtKB: Cytochrome b

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

MacromoleculeName: Cytochrome b-c1 complex subunit Rieske, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 28.545494 KDa
SequenceString: MALRRAVASF LPKLAGAAET LPAASHAASS FSQLICTPLD VVERQQQPSG FRSFASDAVE VFKPETGLTP TNRLSMAPTP YIKYDEHNH KRFPPGTEGR PFAYFVQTGG RFLYASAARL AVLKIVMSLS AAADTMALSS LEVDLSGVEE GTTITVKWRG K PVFIRHRT ...String:
MALRRAVASF LPKLAGAAET LPAASHAASS FSQLICTPLD VVERQQQPSG FRSFASDAVE VFKPETGLTP TNRLSMAPTP YIKYDEHNH KRFPPGTEGR PFAYFVQTGG RFLYASAARL AVLKIVMSLS AAADTMALSS LEVDLSGVEE GTTITVKWRG K PVFIRHRT DAEIAQSAEV ALSELRDPQK DVDRAINPKY LVVVGICTHL GCVPISGAGN YQGWFCPCHG SHYDISGRIR EG PAPYNLE VPEYRFTEGQ KVVIG

UniProtKB: Cytochrome b-c1 complex subunit Rieske, mitochondrial

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Macromolecule #3: Cytochrome c1

MacromoleculeName: Cytochrome c1 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 33.868195 KDa
SequenceString: MRTSLLRSLG KGLGLCAEAT SSRVAQQTMP AVAAMSTSAS DAEPTSKAAH YAAALGGVMA GIFGASCVAS ANEAADGLHA PHYPWGHEG VLDSYDHAAI RRGHKVYQQV CAACHSMQYL HWRQLVGVCY TEEEAKALAA ETEVEDGPND EGEMFTREGR L FDAFPSPY ...String:
MRTSLLRSLG KGLGLCAEAT SSRVAQQTMP AVAAMSTSAS DAEPTSKAAH YAAALGGVMA GIFGASCVAS ANEAADGLHA PHYPWGHEG VLDSYDHAAI RRGHKVYQQV CAACHSMQYL HWRQLVGVCY TEEEAKALAA ETEVEDGPND EGEMFTREGR L FDAFPSPY ANEQAARYAN GGAYPPDLTL ISGGRHNGPN YIFSLLTGYR DPPAGISIRE GLYYNPYFPG GAIAMPKMLV DG GVEYEDG TPASASQQAK DITTFLAWAS YPYQDEMRVM GIKACLMISI LIGFAAYSKR LRWAPIKSQR IVMDVVN

UniProtKB: Cytochrome c1

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Macromolecule #4: Complex III subunit 9

MacromoleculeName: Complex III subunit 9 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 7.040211 KDa
SequenceString:
MVMRLSEALY QTFFKRSTVY IPMLLVGAYF SNEAIDYAVD KMWTTRNKGK LFSDIIAERT

UniProtKB: Complex III subunit 9

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Macromolecule #5: Cytochrome b-c1 complex subunit 6

MacromoleculeName: Cytochrome b-c1 complex subunit 6 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 7.991032 KDa
SequenceString:
MVEYTEDDPK PQIEEDCKPH CVKEWAAYKA CAERIKDDTT GQAHCSGQYF DFWKCVDHCA APKIFAHLK

UniProtKB: Cytochrome b-c1 complex subunit 6

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Macromolecule #6: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8

MacromoleculeName: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8
type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 8.678994 KDa
SequenceString:
MAPRQNIPLR EILYQLSPYQ QDVIRQTFTN APKTFLRFFK EKGVGLATFG VLFFGIKGYT EHEMHQERLA ERY

UniProtKB: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 8

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Macromolecule #7: MPP-Beta

MacromoleculeName: MPP-Beta / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 55.121215 KDa
SequenceString: MRSLKQILRI GEASSLGLRA FGSAAKDVVA TDANPFLRFS NPRPSPIDHT PLLSTLPETR ITTLPNGLRV ATEAIPFAET TTLGIWINS GSRFETDANN GVAHFLEHIL FKGTKNRSVK ELEVEVENMG GQLNAYTGRE QTCYYAKVMG KDVGKAVNIL S DILLNSNL ...String:
MRSLKQILRI GEASSLGLRA FGSAAKDVVA TDANPFLRFS NPRPSPIDHT PLLSTLPETR ITTLPNGLRV ATEAIPFAET TTLGIWINS GSRFETDANN GVAHFLEHIL FKGTKNRSVK ELEVEVENMG GQLNAYTGRE QTCYYAKVMG KDVGKAVNIL S DILLNSNL DARAIDKERD VILREMEEVN KQTSELVFDH LHATAFQYSP LGRTILGPVE NIKSINRDQL VEYMKTHYRG PR MVLAAAG AVNHDELVKL ASDAFGSVPD EDAATSVRSL LVKEPSRFTG SYVHDRFPDA SECCMAVAFK GASWTDPDSI PLM VMQTML GGWDKNSTVG KHSSSALVQT VATEGLADAF MAFNTNYHDT GLFGVYGVTD RDRSEDFAYA IMSNLTRMCF EVRD ADVAR AKNQLKASLM FFQDSTHHVA ESIGRELLVY GRRIPKAEMF ARIDAVDANA IRAVADRFIY DQDMAVASAG DVQFV PDYN WFRRRSYWLR Y

UniProtKB: Uncharacterized protein

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Macromolecule #8: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10

MacromoleculeName: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10
type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO / EC number: quinol-cytochrome-c reductase
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 6.476588 KDa
SequenceString:
MPIGVWSVFQ GYVTPARLPS IQTLTRVGAW GGVVVVGGLY MVQPWDWLAV QAGLKKEEK

UniProtKB: Mitochondrial ubiquinol-cytochrome c oxidoreductase subunit 10

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Macromolecule #9: Alpha-MPP

MacromoleculeName: Alpha-MPP / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 49.64043 KDa
SequenceString: MLGSSTSQLA PAMVRSIASS AAASTAAPVL AAKSGGLLAS VFGMGGGRVE VPLSEKLPAV TEPPRTSTPA TKPIVQTSSL RSGVKVASI NTVSPISSLV LFVEGGAAAE TPATAGASKV LEVAAFKATA NRSTFRLTRE LEKIGATSFA RAGRDHVAFG V DATRLNQL ...String:
MLGSSTSQLA PAMVRSIASS AAASTAAPVL AAKSGGLLAS VFGMGGGRVE VPLSEKLPAV TEPPRTSTPA TKPIVQTSSL RSGVKVASI NTVSPISSLV LFVEGGAAAE TPATAGASKV LEVAAFKATA NRSTFRLTRE LEKIGATSFA RAGRDHVAFG V DATRLNQL EALEILADAV VNARYTYWEV RDSLDAVKEQ LAAQLRNPLT AVNEVLHRTA FEGGLGHSLV VDPSVVDGFT NE TLKEYVH SIMAPSRVVL AASGVDHAEL TALATPLLNL HGNAHPAPQS RYVGGAMNII APTSSLTYVG LAFEAKGGAG DIK SSAAAS VVKALLDEAR PTMPYQRKEH EVFTSVNPFA FAYKGTGLVG VVASGAPGKA GKVVDALTAK VQSLAKGVTD VQLA TAKNM ALGELRASVA TAPGLAAAVG SSVLATGKFS ANEVAAALSG LTAADVTSYV NAMIKTAPTF VTYGNLSSLP RVDSI AKRF A

UniProtKB: Uncharacterized protein

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Macromolecule #10: Cytochrome b-c1 complex subunit 7

MacromoleculeName: Cytochrome b-c1 complex subunit 7 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 14.062162 KDa
SequenceString:
MTSLLKQVAL PVFNSLATTY RSVVGAKLAK YGLRFDDLQD PLKDEDVAEA LRRLPPDVVV ARNCRLRRAL DLSCKHEALP KDLLEKQTP ELSYLQDVLN EVRAERRERA QLGAPAPYTR IYYD

UniProtKB: Cytochrome b-c1 complex subunit 7

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

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

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

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Macromolecule #12: HEME C

MacromoleculeName: HEME C / type: ligand / ID: 12 / Number of copies: 6 / Formula: HEC
Molecular weightTheoretical: 618.503 Da
Chemical component information

ChemComp-HEC:
HEME C

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Macromolecule #13: CARDIOLIPIN

MacromoleculeName: CARDIOLIPIN / type: ligand / ID: 13 / Number of copies: 8 / Formula: CDL
Molecular weightTheoretical: 1.464043 KDa
Chemical component information

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

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Macromolecule #14: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE

MacromoleculeName: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE / type: ligand / ID: 14 / Number of copies: 7 / Formula: 3PH
Molecular weightTheoretical: 704.998 Da
Chemical component information

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

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Macromolecule #15: PHOSPHATIDYLETHANOLAMINE

MacromoleculeName: PHOSPHATIDYLETHANOLAMINE / type: ligand / ID: 15 / Number of copies: 2 / Formula: PTY
Molecular weightTheoretical: 734.039 Da
Chemical component information

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

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Macromolecule #16: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5...

MacromoleculeName: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE
type: ligand / ID: 16 / Number of copies: 2 / Formula: PC7
Molecular weightTheoretical: 763.1 Da
Chemical component information

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

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Macromolecule #17: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 17 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #18: water

MacromoleculeName: water / type: ligand / ID: 18 / Number of copies: 538 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
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

Concentration1 mg/mL
BufferpH: 7.5
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 20 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.39 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 83443
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final 3D classificationSoftware - Name: cryoSPARC
FSC plot (resolution estimation)

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