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- EMDB-10318: Complex IV of the III2-IV5B1 respiratory supercomplex from S. cer... -

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Basic information

Entry
Database: EMDB / ID: EMD-10318
TitleComplex IV of the III2-IV5B1 respiratory supercomplex from S. cerevisiae after focused refinement
Map dataNone
Sample
  • Complex: Complex IV of the III2-IV(5B)1 respiratory supercomplex from S. cerevisiae after focused refinement
    • Protein or peptide: x 13 types
Function / homology
Function and homology information


mitochondrial cytochrome c oxidase assembly / matrix side of mitochondrial inner membrane / protein processing involved in protein targeting to mitochondrion / mitochondrial respirasome assembly / Respiratory electron transport / mitochondrial respiratory chain complex III assembly / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / mitochondrial respirasome / cellular respiration ...mitochondrial cytochrome c oxidase assembly / matrix side of mitochondrial inner membrane / protein processing involved in protein targeting to mitochondrion / mitochondrial respirasome assembly / Respiratory electron transport / mitochondrial respiratory chain complex III assembly / mitochondrial respiratory chain complex III / mitochondrial respiratory chain complex IV / mitochondrial respirasome / cellular respiration / cytochrome-c oxidase / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, cytochrome c to oxygen / electron transport coupled proton transport / cytochrome-c oxidase activity / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial crista / ATP synthesis coupled electron transport / enzyme regulator activity / aerobic respiration / proton transmembrane transport / nuclear periphery / mitochondrial membrane / mitochondrial intermembrane space / 2 iron, 2 sulfur cluster binding / metalloendopeptidase activity / mitochondrial inner membrane / oxidoreductase activity / copper ion binding / heme binding / mitochondrion / proteolysis / zinc ion binding / metal ion binding / cytosol
Similarity search - Function
Respiratory supercomplex factor 2, mitochondrial / Hypoxia induced protein, domain / Hypoxia induced protein conserved region / HIG1 domain profile. / Cytochrome c oxidase subunit VII, budding yeast / Cytochrome c oxidase, subunit VIIa, fungal / Cytochrome b-c1 complex subunit 10, fungi / Ubiquinol-cytochrome-c reductase complex subunit (QCR10) / : / Cytochrome c oxidase, subunit VIa, conserved site ...Respiratory supercomplex factor 2, mitochondrial / Hypoxia induced protein, domain / Hypoxia induced protein conserved region / HIG1 domain profile. / Cytochrome c oxidase subunit VII, budding yeast / Cytochrome c oxidase, subunit VIIa, fungal / Cytochrome b-c1 complex subunit 10, fungi / Ubiquinol-cytochrome-c reductase complex subunit (QCR10) / : / Cytochrome c oxidase, subunit VIa, conserved site / Cytochrome c oxidase subunit VIa signature. / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV family / Cytochrome c oxidase subunit VIIc superfamily / Cytochrome c oxidase subunit IV superfamily / Cytochrome c oxidase subunit VIIc / Cytochrome c oxidase subunit IV / Cytochrome c oxidase, subunit VIa / Cytochrome c oxidase, subunit Va/VI / Cytochrome c oxidase, subunit VIa superfamily / Cytochrome c oxidase, subunit Va/VI superfamily / Cytochrome c oxidase subunit VIa / Cytochrome c oxidase subunit Va / Cytochrome c oxidase, subunit VIb / Cytochrome c oxidase, subunit VIb superfamily / Cytochrome oxidase c subunit VIb / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit VII / Cytochrome c oxidase subunit 2, C-terminal / Cytochrome c oxidase subunit III domain / Cytochrome c oxidase subunit Vb, zinc binding region signature. / Cytochrome c oxidase, subunit Vb / Cytochrome c oxidase, subunit Vb superfamily / Cytochrome c oxidase subunit Vb / Cytochrome c oxidase subunit Vb, zinc binding domain profile. / Cytochrome c oxidase subunit I domain / Cytochrome c oxidase, subunit II / Cytochrome C oxidase subunit II, transmembrane domain / 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 c oxidase subunit III / Cytochrome c oxidase subunit III-like / Cytochrome b-c1 complex subunit 9 / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Cytochrome c oxidase subunit III / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Heme-copper oxidase subunit III family profile. / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Cytochrome c oxidase subunit III-like superfamily / 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 C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome b / : / : / Cytochrome c/quinol oxidase subunit II / 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. / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Copper centre Cu(A) / Cytochrome C oxidase subunit II, transmembrane domain superfamily / CO II and nitrous oxide reductase dinuclear copper centers signature. / 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. / Rieske iron-sulphur protein, C-terminal / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Cytochrome C oxidase subunit II, periplasmic domain / Rieske iron-sulphur protein / Cytochrome c oxidase subunit II-like C-terminal / Cytochrome oxidase subunit II copper A binding domain profile. / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like
Similarity search - Domain/homology
Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7, mitochondrial / Cytochrome b / Cytochrome c oxidase subunit 1 / Cytochrome c oxidase subunit 2 / Cytochrome c oxidase subunit 3 / Cytochrome c oxidase subunit 5B, mitochondrial / Cytochrome c oxidase subunit 6, mitochondrial / Cytochrome c oxidase subunit 4, mitochondrial / Cytochrome c oxidase subunit 8, mitochondrial ...Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7, mitochondrial / Cytochrome b / Cytochrome c oxidase subunit 1 / Cytochrome c oxidase subunit 2 / Cytochrome c oxidase subunit 3 / Cytochrome c oxidase subunit 5B, mitochondrial / Cytochrome c oxidase subunit 6, mitochondrial / Cytochrome c oxidase subunit 4, mitochondrial / Cytochrome c oxidase subunit 8, mitochondrial / Cytochrome c1, heme protein, mitochondrial / Cytochrome c oxidase subunit 9, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome b-c1 complex subunit 8, mitochondrial / Cytochrome c oxidase subunit 7, mitochondrial / Cytochrome b-c1 complex subunit 9, mitochondrial / Cytochrome c oxidase subunit 13, mitochondrial / Cytochrome b-c1 complex subunit 10, mitochondrial / Respiratory supercomplex factor 2, mitochondrial / Cytochrome c oxidase subunit 12, mitochondrial / Cytochrome c oxidase subunit 26, mitochondrial
Similarity search - Component
Biological speciesSaccharomyces cerevisiae S288C (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.41 Å
AuthorsMarechal A / Hartley A / Pinotsis N
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Medical Research Council (United Kingdom)MR/M00936X/1 United Kingdom
CitationJournal: Proc Natl Acad Sci U S A / Year: 2020
Title: Rcf2 revealed in cryo-EM structures of hypoxic isoforms of mature mitochondrial III-IV supercomplexes.
Authors: Andrew M Hartley / Brigitte Meunier / Nikos Pinotsis / Amandine Maréchal /
Abstract: The organization of the mitochondrial electron transport chain proteins into supercomplexes (SCs) is now undisputed; however, their assembly process, or the role of differential expression isoforms, ...The organization of the mitochondrial electron transport chain proteins into supercomplexes (SCs) is now undisputed; however, their assembly process, or the role of differential expression isoforms, remain to be determined. In , cytochrome oxidase (CIV) forms SCs of varying stoichiometry with cytochrome (CIII). Recent studies have revealed, in normoxic growth conditions, an interface made exclusively by Cox5A, the only yeast respiratory protein that exists as one of two isoforms depending on oxygen levels. Here we present the cryo-EM structures of the III-IV and III-IV SCs containing the hypoxic isoform Cox5B solved at 3.4 and 2.8 Å, respectively. We show that the change of isoform does not affect SC formation or activity, and that SC stoichiometry is dictated by the level of CIII/CIV biosynthesis. Comparison of the CIV- and CIV-containing SC structures highlighted few differences, found mainly in the region of Cox5. Additional density was revealed in all SCs, independent of the CIV isoform, in a pocket formed by Cox1, Cox3, Cox12, and Cox13, away from the CIII-CIV interface. In the CIV-containing hypoxic SCs, this could be confidently assigned to the hypoxia-induced gene 1 (Hig1) type 2 protein Rcf2. With conserved residues in mammalian Hig1 proteins and Cox3/Cox12/Cox13 orthologs, we propose that Hig1 type 2 proteins are stoichiometric subunits of CIV, at least when within a III-IV SC.
History
DepositionSep 18, 2019-
Header (metadata) releaseApr 22, 2020-
Map releaseApr 22, 2020-
UpdateMay 13, 2020-
Current statusMay 13, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.5
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  • Surface view with fitted model
  • Atomic models: PDB-6t15
  • Surface level: 0.5
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6t15
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10318.png

Downloads & links

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Map

FileDownload / File: emd_10318.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationNone
Voxel sizeX=Y=Z: 1.048 Å
Density
Contour LevelBy AUTHOR: 0.424 / Movie #1: 0.5
Minimum - Maximum-1.3909371 - 3.0042238
Average (Standard dev.)0.009469065 (±0.08076765)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 402.432 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0481.0481.048
M x/y/z384384384
origin x/y/z0.0000.0000.000
length x/y/z402.432402.432402.432
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS384384384
D min/max/mean-1.3913.0040.009

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Supplemental data

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Sample components

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Entire : Complex IV of the III2-IV(5B)1 respiratory supercomplex from S. c...

EntireName: Complex IV of the III2-IV(5B)1 respiratory supercomplex from S. cerevisiae after focused refinement
Components
  • Complex: Complex IV of the III2-IV(5B)1 respiratory supercomplex from S. cerevisiae after focused refinement
    • Protein or peptide: Cox1 Cytochrome c oxidase subunit 1
    • Protein or peptide: Cox2 Cytochrome c oxidase subunit 2
    • Protein or peptide: Cox3 Cytochrome c oxidase subunit 3
    • Protein or peptide: Cox4 Cytochrome c oxidase subunit 4
    • Protein or peptide: Cox5B Cytochrome c oxidase subunit 5B
    • Protein or peptide: Cox6 Cytochrome c oxidase subunit 6
    • Protein or peptide: Cox7 Cytochrome c oxidase subunit 7
    • Protein or peptide: Cox8 Cytochrome c oxidase polypeptide VIII
    • Protein or peptide: Cox9 Cytochrome c oxidase subunit 7A
    • Protein or peptide: Cox12 Cytochrome c oxidase subunit 6B
    • Protein or peptide: Cox13 Cytochrome c oxidase subunit 6A
    • Protein or peptide: Cox26, Uncharacterized protein YDR119W-A
    • Protein or peptide: RCF2, Respiratory supercomplex factor 2, mitochondrial

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Supramolecule #1: Complex IV of the III2-IV(5B)1 respiratory supercomplex from S. c...

SupramoleculeName: Complex IV of the III2-IV(5B)1 respiratory supercomplex from S. cerevisiae after focused refinement
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)

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Macromolecule #1: Cox1 Cytochrome c oxidase subunit 1

MacromoleculeName: Cox1 Cytochrome c oxidase subunit 1 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString: MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLHG NSQLFNVLVV GHAVLMIFF LVMPALIGGF GNYLLPLMIG ATDTAFPRIN NIAFWVLPMG LVCLVTSTLV E SGAGTGWT VYPPLSSIQA HSGPSVDLAI FALHLTSISS LLGAINFIVT ...String:
MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLHG NSQLFNVLVV GHAVLMIFF LVMPALIGGF GNYLLPLMIG ATDTAFPRIN NIAFWVLPMG LVCLVTSTLV E SGAGTGWT VYPPLSSIQA HSGPSVDLAI FALHLTSISS LLGAINFIVT TLNMRTNGMT MH KLPLFVW SIFITAFLLL LSLPVLSAGI TMLLLDRNFN TSFFEVSGGG DPILYEHLFW FFG HPEVYI LIIPGFGIIS HVVSTYSKKP VFGEISMVYA MASIGLLGFL VWSHHMYIVG LDAD TRAYF TSATMIIAIP TGIKIFSWLA TIHGGSIRLA TPMLYAIAFL FLFTMGGLTG VALAN ASLD VAFHDTYYVV GHFHYVLSMG AIFSLFAGYY YWSPQILGLN YNEKLAQIQF WLIFIG ANV IFFPMHFLGI NGMPRRIPDY PDAFAGWNYV ASIGSFIATL SLFLFIYILY DQLVNGL NN KVNNKSVIYN KAPDFVESNT IFNLNTVKSS SIEFLLTSPP AVHSFNTPAV QS

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Macromolecule #2: Cox2 Cytochrome c oxidase subunit 2

MacromoleculeName: Cox2 Cytochrome c oxidase subunit 2 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString: MLDLLRLQLT TFIMNDVPTP YACYFQDSAT PNQEGILELH DNIMFYLLVI LGLVSWMLYT IVMTYSKNP IAYKYIKHGQ TIEVIWTIFP AVILLIIAFP SFILLYLCDE VISPAMTIKA I GYQWYWKY EYSDFINDSG ETVEFESYVI PDELLEEGQL RLLDTDTSMV ...String:
MLDLLRLQLT TFIMNDVPTP YACYFQDSAT PNQEGILELH DNIMFYLLVI LGLVSWMLYT IVMTYSKNP IAYKYIKHGQ TIEVIWTIFP AVILLIIAFP SFILLYLCDE VISPAMTIKA I GYQWYWKY EYSDFINDSG ETVEFESYVI PDELLEEGQL RLLDTDTSMV VPVDTHIRFV VT AADVIHD FAIPSLGIKV DATPGRLNQV SALIQREGVF YGACSELCGT GHANMPIKIE AVS LPKFLE WLNEQ

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Macromolecule #3: Cox3 Cytochrome c oxidase subunit 3

MacromoleculeName: Cox3 Cytochrome c oxidase subunit 3 / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString: MTHLERSRHQ QHPFHMVMPS PWPIVVSFAL LSLALSTALT MHGYIGNMNM VYLALFVLLT SSILWFRDI VAEATYLGDH TMAVRKGINL GFLMFVLSEV LIFAGLFWAY FHSAMSPDVT L GACWPPVG IEAVQPTELP LLNTIILLSS GATVTYSHHA LIAGNRNKAL ...String:
MTHLERSRHQ QHPFHMVMPS PWPIVVSFAL LSLALSTALT MHGYIGNMNM VYLALFVLLT SSILWFRDI VAEATYLGDH TMAVRKGINL GFLMFVLSEV LIFAGLFWAY FHSAMSPDVT L GACWPPVG IEAVQPTELP LLNTIILLSS GATVTYSHHA LIAGNRNKAL SGLLITFWLI VI FVTCQYI EYTNAAFTIS DGVYGSVFYA GTGLHFLHMV MLAAMLGVNY WRMRNYHLTA GHH VGYETT IIYTHVLDVI WLFLYVVFYW WGV

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Macromolecule #4: Cox4 Cytochrome c oxidase subunit 4

MacromoleculeName: Cox4 Cytochrome c oxidase subunit 4 / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString:
MLSLRQSIRF FKPATRTLCS SRYLLQQKPV VKTAQNLAEV NGPETLIGPG AKEGTVPTDL DQETGLARL ELLGKLEGID VFDTKPLDSS RKGTMKDPII IESYDDYRYV GCTGSPAGSH T IMWLKPTV NEVARCWECG SVYKLNPVGV PNDDHHH

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Macromolecule #5: Cox5B Cytochrome c oxidase subunit 5B

MacromoleculeName: Cox5B Cytochrome c oxidase subunit 5B / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString:
MLRTSLTKGA RLTGTRFVQT KALSKATLTD LPERWENMPN LEQKEIADNL TERQKLPWKT LNNEEIKAA WYISYGEWGP RRPVHGKGDV AFITKGVFLG LGISFGLFGL VRLLANPETP K TMNREWQL KSDEYLKSKN ANPWGGYSQV QSK

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Macromolecule #6: Cox6 Cytochrome c oxidase subunit 6

MacromoleculeName: Cox6 Cytochrome c oxidase subunit 6 / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString:
MLSRAIFRNP VINRTLLRAR PGAYHATRLT KNTFIQSRKY SDAHDEETFE EFTARYEKEF DEAYDLFEV QRVLNNCFSY DLVPAPAVIE KALRAARRVN DLPTAIRVFE ALKYKVENED Q YKAYLDEL KDVRQELGVP LKEELFPSSS

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Macromolecule #7: Cox7 Cytochrome c oxidase subunit 7

MacromoleculeName: Cox7 Cytochrome c oxidase subunit 7 / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString:
MANKVIQLQ KIFQSSTKPL WWRHPRSALY LYPFYAIFAV AVVTPLLYIP NAIRGIKAKK A

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Macromolecule #8: Cox8 Cytochrome c oxidase polypeptide VIII

MacromoleculeName: Cox8 Cytochrome c oxidase polypeptide VIII / type: protein_or_peptide / ID: 8 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString:
MLCQQMIRTT AKRSSNIMTR PIIMKRSVHF KDGVYENIPF KVKGRKTPYA LSHFGFFAIG FAVPFVACY VQLKKSGAF

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Macromolecule #9: Cox9 Cytochrome c oxidase subunit 7A

MacromoleculeName: Cox9 Cytochrome c oxidase subunit 7A / type: protein_or_peptide / ID: 9 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString:
MTIAPITGTI KRRVIMDIVL GFSLGGVMAS YWWWGFHMDK INKREKFYAE LAERKKQEN

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Macromolecule #10: Cox12 Cytochrome c oxidase subunit 6B

MacromoleculeName: Cox12 Cytochrome c oxidase subunit 6B / type: protein_or_peptide / ID: 10 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString:
MADQENSPLH TVGFDARFPQ QNQTKHCWQS YVDYHKCVNM KGEDFAPCKV FWKTYNALCP LDWIEKWDD QREKGIFAGD INSD

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Macromolecule #11: Cox13 Cytochrome c oxidase subunit 6A

MacromoleculeName: Cox13 Cytochrome c oxidase subunit 6A / type: protein_or_peptide / ID: 11 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString:
MFRQCAKRYA SSLPPNALKP AFGPPDKVAA QKFKESLMAT EKHAKDTSNM WVKISVWVAL PAIALTAVN TYFVEKEHAE HREHLKHVPD SEWPRDYEFM NIRSKPFFWG DGDKTLFWNP V VNRHIEHD DGARGSHHHH HH

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Macromolecule #12: Cox26, Uncharacterized protein YDR119W-A

MacromoleculeName: Cox26, Uncharacterized protein YDR119W-A / type: protein_or_peptide / ID: 12 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString:
MFFSQVLRSS ARAAPIKRYT GGRIGESWVI TEGRRLIPEI FQWSAVLSVC LGWPGAVYFF SKARKA

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Macromolecule #13: RCF2, Respiratory supercomplex factor 2, mitochondrial

MacromoleculeName: RCF2, Respiratory supercomplex factor 2, mitochondrial
type: protein_or_peptide / ID: 13 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
SequenceString: MKILTQDEIE AHRSHTLKGG IEGALAGFAI SAIIFKVLPR RYPKFKPSTL TWSIKTALWI TPPTVLTAI CAEEASNNFD ATMYGSGSSS EDALDEHRRW KSLSTKDKFV EGLSNNKYKI I TGAWAASL YGSWVIVNKD PIMTKAQKIV QARMYAQFIT VGLLLASVGL ...String:
MKILTQDEIE AHRSHTLKGG IEGALAGFAI SAIIFKVLPR RYPKFKPSTL TWSIKTALWI TPPTVLTAI CAEEASNNFD ATMYGSGSSS EDALDEHRRW KSLSTKDKFV EGLSNNKYKI I TGAWAASL YGSWVIVNKD PIMTKAQKIV QARMYAQFIT VGLLLASVGL SMYENKLHPN KQ KVNEMRR WENALRVAEE EERLEKEGRR TGYVSNEERI NSKIFKS

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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: 7.2
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV
Details: 3 microliter of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec..

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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
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 56.4 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: cryoSPARC (ver. 2)
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 2)
Final 3D classificationSoftware - Name: cryoSPARC (ver. 2)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 2)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.41 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 2)
Details: Particle subtraction from CIII2-CIV15B particles and focused refinement on CIV
Number images used: 73042
FSC plot (resolution estimation)

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