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- EMDB-50205: Structure of the Chlamydomonas reinhardtii respiratory complex IV... -

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Basic information

Entry
Database: EMDB / ID: EMD-50205
TitleStructure of the Chlamydomonas reinhardtii respiratory complex IV from respiratory supercomplex
Map data
Sample
  • Complex: Small subunit of the flowering plant mitochondrial ribosome in presence of RsgA
    • Protein or peptide: x 12 types
  • Ligand: x 8 types
Keywordsmitochondria / mitoribosome / assembly factor / plant / RIBOSOME / MEMBRANE PROTEIN
Function / homology
Function and homology information


respiratory chain complex IV / mitochondrial envelope / cytochrome-c oxidase / oxidative phosphorylation / mitochondrial electron transport, cytochrome c to oxygen / cytochrome-c oxidase activity / proton transmembrane transport / electron transport chain / mitochondrial inner membrane / copper ion binding ...respiratory chain complex IV / mitochondrial envelope / cytochrome-c oxidase / oxidative phosphorylation / mitochondrial electron transport, cytochrome c to oxygen / cytochrome-c oxidase activity / proton transmembrane transport / electron transport chain / mitochondrial inner membrane / copper ion binding / heme binding / mitochondrion / metal ion binding / membrane
Similarity search - Function
Cytochrome c oxidase, subunit VIb / : / Cytochrome c oxidase, subunit VIb superfamily / Cytochrome c oxidase subunit 2, C-terminal / Cytochrome oxidase c subunit VIb / Cytochrome c oxidase subunit III domain / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome c oxidase subunit I domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome C oxidase subunit II, transmembrane domain ...Cytochrome c oxidase, subunit VIb / : / Cytochrome c oxidase, subunit VIb superfamily / Cytochrome c oxidase subunit 2, C-terminal / Cytochrome oxidase c subunit VIb / Cytochrome c oxidase subunit III domain / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome c oxidase subunit I domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome c oxidase subunit III / Cytochrome c oxidase subunit III-like / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome c oxidase subunit III / Heme-copper oxidase subunit III family profile. / Cytochrome c oxidase subunit III-like superfamily / Cytochrome c/quinol oxidase subunit II / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / Cytochrome C oxidase subunit II, transmembrane domain superfamily / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / Cytochrome C oxidase subunit II, periplasmic domain / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Cytochrome c oxidase subunit II-like C-terminal / Cytochrome oxidase subunit II copper A binding domain profile. / Coiled coil-helix-coiled coil-helix (CHCH) domain profile. / Cupredoxin
Similarity search - Domain/homology
Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Cytochrome c oxidase subunit 1 / Cytochrome c oxidase subunit / cytochrome-c oxidase ...Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Cytochrome c oxidase subunit 1 / Cytochrome c oxidase subunit / cytochrome-c oxidase / Cytochrome c oxidase polypeptide II / Cytochrome c oxidase subunit 3
Similarity search - Component
Biological speciesBrassica oleracea var. botrytis (cauliflower) / Chlamydomonas 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_50205.png

Downloads & links

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Map

FileDownload / File: emd_50205.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

Projections

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.00272 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.135
Minimum - Maximum-0.45284176 - 0.84964985
Average (Standard dev.)0.000052450076 (±0.019958718)
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_50205_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_50205_half_map_1.map
Projections & Slices
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Histogram

Histogram (log scale)

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Half map: #1

Fileemd_50205_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : Small subunit of the flowering plant mitochondrial ribosome in pr...

EntireName: Small subunit of the flowering plant mitochondrial ribosome in presence of RsgA
Components
  • Complex: Small subunit of the flowering plant mitochondrial ribosome in presence of RsgA
    • Protein or peptide: Cytochrome c oxidase subunit 1
    • Protein or peptide: Cytochrome c oxidase polypeptide II
    • Protein or peptide: cytochrome-c oxidase
    • Protein or peptide: Cytochrome c oxidase subunit 3
    • Protein or peptide: Cox5b
    • Protein or peptide: Cox5c
    • Protein or peptide: Cox6a
    • Protein or peptide: Cox6b
    • Protein or peptide: Cox7c
    • Protein or peptide: Cytochrome c oxidase subunit
    • Protein or peptide: Cox7a
    • Protein or peptide: CoxIn
  • Ligand: HEME-A
  • Ligand: COPPER (II) ION
  • Ligand: MAGNESIUM ION
  • Ligand: (7S)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE
  • Ligand: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE
  • Ligand: DINUCLEAR COPPER ION
  • Ligand: PHOSPHATIDYLETHANOLAMINE
  • Ligand: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE

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Supramolecule #1: Small subunit of the flowering plant mitochondrial ribosome in pr...

SupramoleculeName: Small subunit of the flowering plant mitochondrial ribosome in presence of RsgA
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#12
Source (natural)Organism: Brassica oleracea var. botrytis (cauliflower)

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Macromolecule #1: Cytochrome c oxidase subunit 1

MacromoleculeName: Cytochrome c oxidase subunit 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: cytochrome-c oxidase
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 55.194918 KDa
SequenceString: MRWLYSTSHK DIGLLYLVFA FFGGLLGTSL SMLIRYELAL PGRGLLDGNG QLYNVIITGH GIIMLLFMVM PALFGGFGNW LLPIMIGAP DMAFPRLNNI SFWLNPPALA LLLLSTLVEQ GPGTGWTAYP PLSVQHSGTS VDLAILSLHL NGLSSILGAV N MLVTVAGL ...String:
MRWLYSTSHK DIGLLYLVFA FFGGLLGTSL SMLIRYELAL PGRGLLDGNG QLYNVIITGH GIIMLLFMVM PALFGGFGNW LLPIMIGAP DMAFPRLNNI SFWLNPPALA LLLLSTLVEQ GPGTGWTAYP PLSVQHSGTS VDLAILSLHL NGLSSILGAV N MLVTVAGL RAPGMKLLHM PLFVWAIALT AVLVILAVPV LAAALVMLLT DRNINTAYFC ESGDLILYQH LFWFFGHPEV YI LILPAFG IVSQVVSFFS QKPVFGLTGM ICAMGAISLL GFIVWAHHMF TVGLDLDTVA YFTSATMIIA VPTGMKIFSW MAT IYSGRV WFTTPMWFAV GFICLFTLGG VTGVVLANAG VDMLVHDTYY VVAHFHYVLS MGAVFGIFAG VYFWGNLITG LGYH EGRAM VHFWLLFIGV NLTFFPQHFL GLAGMPRRMF DYADCFAGWN AVSSFGASIS FISVIVFATT FQEAVRTVPR TATTL EWVL LATPAHHALS QVPVLRTASS H

UniProtKB: Cytochrome c oxidase subunit 1

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Macromolecule #2: Cytochrome c oxidase polypeptide II

MacromoleculeName: Cytochrome c oxidase polypeptide II / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 30.716742 KDa
SequenceString: MLRQSGLSAN KLFCSNLLQS QQKEGNKLVW NAMLFSSKAE GSAVQQVVAS EGVAQAVPQF SSEAAAALAA KRRGLIGSGM SLAPSKPFA ARGLTSAAKP AAAAAAGAAE AAQPADKYAG LKKVLKAAAA LAAALGLTTT TAAADSPQPW QLLFQDTATS T AQAMIDLH ...String:
MLRQSGLSAN KLFCSNLLQS QQKEGNKLVW NAMLFSSKAE GSAVQQVVAS EGVAQAVPQF SSEAAAALAA KRRGLIGSGM SLAPSKPFA ARGLTSAAKP AAAAAAGAAE AAQPADKYAG LKKVLKAAAA LAAALGLTTT TAAADSPQPW QLLFQDTATS T AQAMIDLH HDIFFFLITV VTLVFYMMFQ IITKFHYSKV LKPEKLTHHT TMEVIWTIIP TLIVVMIAIP SLTLIYSLDQ HT ERPGLTV KIIGRQWYWS YEMHDHLQHK LLDPDRLVGI AEKALVK

UniProtKB: Cytochrome c oxidase polypeptide II

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Macromolecule #3: cytochrome-c oxidase

MacromoleculeName: cytochrome-c oxidase / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: cytochrome-c oxidase
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 17.270035 KDa
SequenceString:
MSESKDQLKE KLKADPSFRA ELKDRIKNAL LSKVPASVPI SYNFDSYMLT EVQPGQLRVL EVDERLVLPT NTLIRLLVTA SDVLHSWAV PALGVKMDAV PGRLNQVWMS INREGVFYGQ CSELCGANHS FMPIVVEAIS PRQFLTEYVK KWIS

UniProtKB: cytochrome-c oxidase

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Macromolecule #4: Cytochrome c oxidase subunit 3

MacromoleculeName: Cytochrome c oxidase subunit 3 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 41.453922 KDa
SequenceString: MRSQLLRFLT RAPAGFSQEG LQALRAGLTS GEASGLLQSS AFGRQNESAA PRGLGFGKMA LPLSFQGHLM STLASANGDD KKEPTTGAL AQQPQVPNAL AALPPRGTRT MGSHAAGHQT AKEFYMEHIG KRHPFHVLPP SPWPMLAGWG TYVSCLGMAA W FHNMPTGG ...String:
MRSQLLRFLT RAPAGFSQEG LQALRAGLTS GEASGLLQSS AFGRQNESAA PRGLGFGKMA LPLSFQGHLM STLASANGDD KKEPTTGAL AQQPQVPNAL AALPPRGTRT MGSHAAGHQT AKEFYMEHIG KRHPFHVLPP SPWPMLAGWG TYVSCLGMAA W FHNMPTGG ALMAFGMANI AWTAITWWRD CAIEGDMGMH TEVVRKNFIS GMWAFIVSEA LLFVGLLWAC LHLGMSPSVA LQ MQWPPVG IEPIGWDKRA LVMSAVLAAS YYSANVAMVA KDPKVVMGAL ATTIGLGAMF LADQYLEYNE TPFTITDSPY GTT FFVTTG FHGMHVLLGS LYLTAALMMY KRTHNAGAAL KSSILYWHFV DIVWIAVYGI IYVGQY

UniProtKB: Cytochrome c oxidase subunit 3

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Macromolecule #5: Cox5b

MacromoleculeName: Cox5b / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 19.051588 KDa
SequenceString:
MNRLGALSGL LARAARTCSR RWATAASGVP AELSAVGIVG QEFAAQARSL HTSLTTCQGA PAEAKPSALS AEPPRKYRPL GDKELWHEA WMYEDKFGTE EDPIIVPSLE AERIIGVTDP EDETLVVWGI LKDGEPPRQF VENGEFYVLK HVEYIKKVGD V LEAIEGGA DKAKIAK

UniProtKB: Uncharacterized protein

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Macromolecule #6: Cox5c

MacromoleculeName: Cox5c / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 10.886307 KDa
SequenceString:
MSQAPATAAS KAVYAPSEYF KYGEGASKHF GFAKHVAIAM TVGLGLSFAW KTWHWNEKRY IAQYYADMAR REAREDAARK SALADKYKQ LEEELLS

UniProtKB: Uncharacterized protein

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Macromolecule #7: Cox6a

MacromoleculeName: Cox6a / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 13.985016 KDa
SequenceString:
MQALRRAVST AMPGFRRAST TAGETIDKYW APYFPKPAVT ADEAKKSVNK EMVGFMLLGP VGVAFMLYDF AVGLEEEHHV TIPPYPWMR IRRLPGMPWG QDGLFEGHPR VATTWPPEEG AADSHH

UniProtKB: Uncharacterized protein

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Macromolecule #8: Cox6b

MacromoleculeName: Cox6b / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 17.277316 KDa
SequenceString:
MGLFNYFVAR ADAEVVEEEH APPPPPPPPK KSSRKPTLES LSADELEELK NEVVSEVVDK IAGEDGTKLA DFLEPELITA PYDPRFPNR NQARHCFVRF NEYYKCLYER GEEHPRCQFY QKAYQSLCPS EWVESWQELR EKGLWTGKY

UniProtKB: Uncharacterized protein

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Macromolecule #9: Cox7c

MacromoleculeName: Cox7c / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 11.356865 KDa
SequenceString:
MSSALRRLSQ QAPRLTRGLK TGNVTKGGAE KYSHEEVVYG DGHHGLRKGY TYDFEHGPHY LQPEKIPNFW SKFYAGTGAL YAVGLGVPL FAVWWQQSKL KA

UniProtKB: Uncharacterized protein

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Macromolecule #10: Cytochrome c oxidase subunit

MacromoleculeName: Cytochrome c oxidase subunit / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 11.694374 KDa
SequenceString:
MARAQIERWA AEHPTAPRVG RIFEVPLGYV VPRVAAGIAA AGCLWYMNNT FLQTYRPESL SKEFLEEQAK IGEVAQRMNA PPVYLNPFT NRIPGSILGP EDAKPE

UniProtKB: Cytochrome c oxidase subunit

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Macromolecule #11: Cox7a

MacromoleculeName: Cox7a / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 6.53242 KDa
SequenceString:
MFPSRALKAA ADSYKATDFT NPKYNYFFRE LTARVQGVLL TGGSLYGTWL VVFGEAQR

UniProtKB: Uncharacterized protein

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Macromolecule #12: CoxIn

MacromoleculeName: CoxIn / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Molecular weightTheoretical: 9.905305 KDa
SequenceString:
MPLPFKLPLD AYILMLPITY ASAAFVAMCC RVPTADPETS SIAYYEDEQK SAAAAQRYDN SFKQFFDARI RNHKVGVFQN WMPNSPQ

UniProtKB: Uncharacterized protein

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Macromolecule #13: HEME-A

MacromoleculeName: HEME-A / type: ligand / ID: 13 / Number of copies: 2 / Formula: HEA
Molecular weightTheoretical: 852.837 Da
Chemical component information

ChemComp-HEA:
HEME-A

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Macromolecule #14: COPPER (II) ION

MacromoleculeName: COPPER (II) ION / type: ligand / ID: 14 / Number of copies: 1 / Formula: CU
Molecular weightTheoretical: 63.546 Da
Chemical component information

ChemComp-CU:
COPPER (II) ION

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Macromolecule #15: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 15 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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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: 1 / 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: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...

MacromoleculeName: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE
type: ligand / ID: 17 / Number of copies: 1 / Formula: PGT
Molecular weightTheoretical: 751.023 Da
Chemical component information

ChemComp-PGT:
(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipid*YM

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Macromolecule #18: DINUCLEAR COPPER ION

MacromoleculeName: DINUCLEAR COPPER ION / type: ligand / ID: 18 / Number of copies: 1 / Formula: CUA
Molecular weightTheoretical: 127.092 Da
Chemical component information

ChemComp-CUA:
DINUCLEAR COPPER ION

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Macromolecule #19: PHOSPHATIDYLETHANOLAMINE

MacromoleculeName: PHOSPHATIDYLETHANOLAMINE / type: ligand / ID: 19 / Number of copies: 2 / Formula: PTY
Molecular weightTheoretical: 734.039 Da
Chemical component information

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

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Macromolecule #20: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE

MacromoleculeName: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE / type: ligand / ID: 20 / Number of copies: 2 / Formula: 3PH
Molecular weightTheoretical: 704.998 Da
Chemical component information

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

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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

Concentration3 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

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 36.27 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 165000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 553666
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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Atomic model buiding 1

RefinementSpace: REAL
Output model

PDB-9f60:
Structure of the Chlamydomonas reinhardtii respiratory complex IV from respiratory supercomplex

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