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- EMDB-11774: Cryo-EM structure of the signal sequence-engaged post-translation... -

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Basic information

Entry
Database: EMDB / ID: EMD-11774
TitleCryo-EM structure of the signal sequence-engaged post-translational Sec translocon
Map data
Sample
  • Complex: Signal sequence-engaged post-translational Sec translocon
    • Complex: Signal sequence-engaged post-translational Sec translocon
      • Protein or peptide: Protein transport protein SEC61Protein targeting
      • Protein or peptide: Protein transport protein SBH1Protein targeting
      • Protein or peptide: Protein transport protein SSS1Protein targeting
      • Protein or peptide: Protein translocation protein SEC63Protein targeting
      • Protein or peptide: Translocation protein SEC66
      • Protein or peptide: Translocation protein SEC72
    • Complex: Translocation protein SEC62
      • Protein or peptide: Translocation protein SEC62,Translocation protein SEC62
    • Complex: Mating factor alpha-1
      • Protein or peptide: Mating factor alpha-1,Mating factor alpha-1
Function / homology
Function and homology information


mating pheromone activity / mating / protein transmembrane import into intracellular organelle / misfolded protein transport / pheromone-dependent signal transduction involved in conjugation with cellular fusion / Sec62/Sec63 complex / translocon complex / cytosol to endoplasmic reticulum transport / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / rough endoplasmic reticulum membrane ...mating pheromone activity / mating / protein transmembrane import into intracellular organelle / misfolded protein transport / pheromone-dependent signal transduction involved in conjugation with cellular fusion / Sec62/Sec63 complex / translocon complex / cytosol to endoplasmic reticulum transport / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / rough endoplasmic reticulum membrane / Ssh1 translocon complex / Sec61 translocon complex / protein-transporting ATPase activity / post-translational protein targeting to endoplasmic reticulum membrane / filamentous growth / SRP-dependent cotranslational protein targeting to membrane, translocation / peptide transmembrane transporter activity / signal sequence binding / SRP-dependent cotranslational protein targeting to membrane / post-translational protein targeting to membrane, translocation / cupric ion binding / nuclear inner membrane / retrograde protein transport, ER to cytosol / protein transmembrane transporter activity / : / guanyl-nucleotide exchange factor activity / cell periphery / ribosome binding / endoplasmic reticulum membrane / structural molecule activity / endoplasmic reticulum / mitochondrion / extracellular region / membrane / cytosol
Similarity search - Function
Translocation protein Sec62, ascomycota / Translocation protein Sec62 / Translocation protein Sec62 / Mating factor alpha, C-terminal repeat / Mating factor alpha precursor, N-terminal / Yeast mating factor alpha hormone / Mating factor alpha precursor N-terminus / Translocation protein Sec66 / Preprotein translocase subunit Sec66 / Protein transport Sec61-beta/Sbh ...Translocation protein Sec62, ascomycota / Translocation protein Sec62 / Translocation protein Sec62 / Mating factor alpha, C-terminal repeat / Mating factor alpha precursor, N-terminal / Yeast mating factor alpha hormone / Mating factor alpha precursor N-terminus / Translocation protein Sec66 / Preprotein translocase subunit Sec66 / Protein transport Sec61-beta/Sbh / Protein transport protein SecG/Sec61-beta/Sbh / Sec61beta family / Protein translocase SEC61 complex, gamma subunit / Protein translocase SecE domain superfamily / Translocon Sec61/SecY, plug domain / Plug domain of Sec61p / Nt-dnaJ domain signature. / DnaJ domain, conserved site / Protein secE/sec61-gamma signature. / Protein secY signature 1. / Protein secY signature 2. / SecE/Sec61-gamma subunits of protein translocation complex / Protein translocase complex, SecE/Sec61-gamma subunit / SecY/SEC61-alpha family / SecY domain superfamily / SecY conserved site / SecY / Sec63 domain / Sec63 Brl domain / DnaJ domain / DnaJ molecular chaperone homology domain / dnaJ domain profile. / Chaperone J-domain superfamily / DnaJ domain / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily / Immunoglobulin E-set
Similarity search - Domain/homology
Mating factor alpha-1 / Protein translocation protein SEC63 / Translocation protein SEC62 / Protein transport protein SEC61 / Translocation protein SEC66 / Protein transport protein SSS1 / Translocation protein SEC72 / Protein transport protein SBH1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) / Baker's yeast (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.4 Å
AuthorsWeng T-H / Beatrix B / Berninghausen O / Becker T / Cheng J / Beckmann R
CitationJournal: EMBO J / Year: 2021
Title: Architecture of the active post-translational Sec translocon.
Authors: Tsai-Hsuan Weng / Wieland Steinchen / Birgitta Beatrix / Otto Berninghausen / Thomas Becker / Gert Bange / Jingdong Cheng / Roland Beckmann /
Abstract: In eukaryotes, most secretory and membrane proteins are targeted by an N-terminal signal sequence to the endoplasmic reticulum, where the trimeric Sec61 complex serves as protein-conducting channel ...In eukaryotes, most secretory and membrane proteins are targeted by an N-terminal signal sequence to the endoplasmic reticulum, where the trimeric Sec61 complex serves as protein-conducting channel (PCC). In the post-translational mode, fully synthesized proteins are recognized by a specialized channel additionally containing the Sec62, Sec63, Sec71, and Sec72 subunits. Recent structures of this Sec complex in the idle state revealed the overall architecture in a pre-opened state. Here, we present a cryo-EM structure of the yeast Sec complex bound to a substrate, and a crystal structure of the Sec62 cytosolic domain. The signal sequence is inserted into the lateral gate of Sec61α similar to previous structures, yet, with the gate adopting an even more open conformation. The signal sequence is flanked by two Sec62 transmembrane helices, the cytoplasmic N-terminal domain of Sec62 is more rigidly positioned, and the plug domain is relocated. We crystallized the Sec62 domain and mapped its interaction with the C-terminus of Sec63. Together, we obtained a near-complete and integrated model of the active Sec complex.
History
DepositionSep 20, 2020-
Header (metadata) releaseDec 2, 2020-
Map releaseDec 2, 2020-
UpdateFeb 10, 2021-
Current statusFeb 10, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.02
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  • Surface view colored by height
  • Surface level: 0.02
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  • Surface view with fitted model
  • Atomic models: PDB-7aft
  • Surface level: 0.02
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7aft
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11774.png

Downloads & links

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Map

FileDownload / File: emd_11774.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.059 Å
Density
Contour LevelBy AUTHOR: 0.018 / Movie #1: 0.02
Minimum - Maximum-0.048339542 - 0.091499545
Average (Standard dev.)0.0004280783 (±0.004853368)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 211.8 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0591.0591.059
M x/y/z200200200
origin x/y/z0.0000.0000.000
length x/y/z211.800211.800211.800
α/β/γ90.00090.00090.000
start NX/NY/NZ79740
NX/NY/NZ93103213
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS200200200
D min/max/mean-0.0480.0910.000

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Supplemental data

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Sample components

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Entire : Signal sequence-engaged post-translational Sec translocon

EntireName: Signal sequence-engaged post-translational Sec translocon
Components
  • Complex: Signal sequence-engaged post-translational Sec translocon
    • Complex: Signal sequence-engaged post-translational Sec translocon
      • Protein or peptide: Protein transport protein SEC61Protein targeting
      • Protein or peptide: Protein transport protein SBH1Protein targeting
      • Protein or peptide: Protein transport protein SSS1Protein targeting
      • Protein or peptide: Protein translocation protein SEC63Protein targeting
      • Protein or peptide: Translocation protein SEC66
      • Protein or peptide: Translocation protein SEC72
    • Complex: Translocation protein SEC62
      • Protein or peptide: Translocation protein SEC62,Translocation protein SEC62
    • Complex: Mating factor alpha-1
      • Protein or peptide: Mating factor alpha-1,Mating factor alpha-1

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Supramolecule #1: Signal sequence-engaged post-translational Sec translocon

SupramoleculeName: Signal sequence-engaged post-translational Sec translocon
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Molecular weightTheoretical: 255 KDa

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Supramolecule #2: Signal sequence-engaged post-translational Sec translocon

SupramoleculeName: Signal sequence-engaged post-translational Sec translocon
type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#6
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)

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Supramolecule #3: Translocation protein SEC62

SupramoleculeName: Translocation protein SEC62 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #7
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #4: Mating factor alpha-1

SupramoleculeName: Mating factor alpha-1 / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #8
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)

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Macromolecule #1: Protein transport protein SEC61

MacromoleculeName: Protein transport protein SEC61 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 52.978148 KDa
SequenceString: MSSNRVLDLF KPFESFLPEV IAPERKVPYN QKLIWTGVSL LIFLILGQIP LYGIVSSETS DPLYWLRAML ASNRGTLLEL GVSPIITSS MIFQFLQGTQ LLQIRPESKQ DRELFQIAQK VCAIILILGQ ALVVVMTGNY GAPSDLGLPI CLLLIFQLMF A SLIVMLLD ...String:
MSSNRVLDLF KPFESFLPEV IAPERKVPYN QKLIWTGVSL LIFLILGQIP LYGIVSSETS DPLYWLRAML ASNRGTLLEL GVSPIITSS MIFQFLQGTQ LLQIRPESKQ DRELFQIAQK VCAIILILGQ ALVVVMTGNY GAPSDLGLPI CLLLIFQLMF A SLIVMLLD ELLSKGYGLG SGISLFTATN IAEQIFWRAF APTTVNSGRG KEFEGAVIAF FHLLAVRKDK KRALVEAFYR TN LPNMFQV LMTVAIFLFV LYLQGFRYEL PIRSTKVRGQ IGIYPIKLFY TSNTPIMLQS ALTSNIFLIS QILFQKYPTN PLI RLIGVW GIRPGTQGPQ MALSGLAYYI QPLMSLSEAL LDPIKTIVYI TFVLGSCAVF SKTWIEISGT SPRDIAKQFK DQGM VINGK RETSIYRELK KIIPTAAAFG GATIGALSVG SDLLGTLGSG ASILMATTTI YGYYEAAAKE GGFTKNLVPG FSDLM

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Macromolecule #2: Protein transport protein SBH1

MacromoleculeName: Protein transport protein SBH1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 8.723155 KDa
SequenceString:
MSSPTPPGGQ RTLQKRKQGS SQKVAASAPK KNTNSNNSIL KIYSDEATGL RVDPLVVLFL AVGFIFSVVA LHVISKVAGK LF

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Macromolecule #3: Protein transport protein SSS1

MacromoleculeName: Protein transport protein SSS1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 8.958641 KDa
SequenceString:
MARASEKGEE KKQSNNQVEK LVEAPVEFVR EGTQFLAKCK KPDLKEYTKI VKAVGIGFIA VGIIGYAIKL IHIPIRYVIV

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Macromolecule #4: Protein translocation protein SEC63

MacromoleculeName: Protein translocation protein SEC63 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 75.432258 KDa
SequenceString: MPTNYEYDEA SETWPSFILT GLLMVVGPMT LLQIYQIFFG ANAEDGNSGK SKEFNEEVFK NLNEEYTSDE IKQFRRKFDK NSNKKSKIW SRRNIIIIVG WILVAILLQR INSNDAIKDA ATKLFDPYEI LGISTSASDR DIKSAYRKLS VKFHPDKLAK G LTPDEKSV ...String:
MPTNYEYDEA SETWPSFILT GLLMVVGPMT LLQIYQIFFG ANAEDGNSGK SKEFNEEVFK NLNEEYTSDE IKQFRRKFDK NSNKKSKIW SRRNIIIIVG WILVAILLQR INSNDAIKDA ATKLFDPYEI LGISTSASDR DIKSAYRKLS VKFHPDKLAK G LTPDEKSV MEETYVQITK AYESLTDELV RQNYLKYGHP DGPQSTSHGI ALPRFLVDGS ASPLLVVCYV ALLGLILPYF VS RWWARTQ SYTKKGIHNV TASNFVSNLV NYKPSEIVTT DLILHWLSFA HEFKQFFPDL QPTDFEKLLQ DHINRRDSGK LNN AKFRIV AKCHSLLHGL LDIACGFRNL DIALGAINTF KCIVQAVPLT PNCQILQLPN VDKEHFITKT GDIHTLGKLF TLED AKIGE VLGIKDQAKL NETLRVASHI PNLKIIKADF LVPGENQVTP SSTPYISLKV LVRSAKQPLI PTSLIPEENL TEPQD FESQ RDPFAMMSKQ PLVPYSFAPF FPTKRRGSWC CLVSSQKDGK ILQTPIIIEK LSYKNLNDDK DFFDKRIKMD LTKHEK FDI NDWEIGTIKI PLGQPAPETV GDFFFRVIVK STDYFTTDLD ITMNMKVRDS PAVEQVEVYS EEDDEYSTDD DETESDD ES DASDYTDIDT DTEAEDDESP E

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Macromolecule #5: Translocation protein SEC66

MacromoleculeName: Translocation protein SEC66 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 24.263939 KDa
SequenceString: MSEFNETKFS NNGTFFETEE PIVETKSISV YTPLIYVFIL VVSLVMFASS YRKKQAKKIS EQPSIFDEND AHDLYFQIKE MSENEKIHE KVLKAALLNR GAESVRRSLK LKELAPQINL LYKNGSIGED YWKRFETEVK LIELEFKDTL QEAERLQPGW V QLFVMVCK ...String:
MSEFNETKFS NNGTFFETEE PIVETKSISV YTPLIYVFIL VVSLVMFASS YRKKQAKKIS EQPSIFDEND AHDLYFQIKE MSENEKIHE KVLKAALLNR GAESVRRSLK LKELAPQINL LYKNGSIGED YWKRFETEVK LIELEFKDTL QEAERLQPGW V QLFVMVCK EICFNQALSR RYQSILKRKE VCIKEWELKI NNDGRLVN

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Macromolecule #6: Translocation protein SEC72

MacromoleculeName: Translocation protein SEC72 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 21.63109 KDa
SequenceString: MVTLEYNANS KLITASDAVV ALSTETNIDQ INVLTTSLIG ETNPNFTPQP NEALSKMIKG LFESGMKNLQ QKKLNEALKN VSLAIEMAQ RKRAPWEAFA IQLPELHFML RSKIDLCLIL GKHLEALQDL DFLLGTGLIQ PDVFVRKADC LLKLRQWEEA R ATCERGLA ...String:
MVTLEYNANS KLITASDAVV ALSTETNIDQ INVLTTSLIG ETNPNFTPQP NEALSKMIKG LFESGMKNLQ QKKLNEALKN VSLAIEMAQ RKRAPWEAFA IQLPELHFML RSKIDLCLIL GKHLEALQDL DFLLGTGLIQ PDVFVRKADC LLKLRQWEEA R ATCERGLA LAPEDMKLRA LLIETARNLA EYNGE

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Macromolecule #7: Translocation protein SEC62,Translocation protein SEC62

MacromoleculeName: Translocation protein SEC62,Translocation protein SEC62
type: protein_or_peptide / ID: 7
Details: The residue numbering in chain G is based on the transmembrane helix prediction of Sec62.
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 35.649891 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString: MSAVGPGSNA GASVNGGSAT AIATLLRNHK ELKQRQGLFQ AKQTDFFRYK RFVRALHSEE YANKSARQPE IYPTIPSNKI EDQLKSREI FIQLIKAQMV IPVKKLHSQE CKEHGLKPSK DFPHLIVSNK AQLEADEYFV WNYNPRTYMD YLIVIGVVSI I LALVCYPL ...String:
MSAVGPGSNA GASVNGGSAT AIATLLRNHK ELKQRQGLFQ AKQTDFFRYK RFVRALHSEE YANKSARQPE IYPTIPSNKI EDQLKSREI FIQLIKAQMV IPVKKLHSQE CKEHGLKPSK DFPHLIVSNK AQLEADEYFV WNYNPRTYMD YLIVIGVVSI I LALVCYPL WPRSMRRGSY YVSLGAFGIL AGFFAVAILR LILYVLSLIV YKDVGGFWIF PNLFEDCGVL ESFKPLYGFG EK DTYSYKK KLKRMKKKQA KRESNKKKAI NEKAEQN(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #8: Mating factor alpha-1,Mating factor alpha-1

MacromoleculeName: Mating factor alpha-1,Mating factor alpha-1 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 19.766402 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MRFPSIFTAV LFAASSALAA PVNTTTEDET AQIPAEAVIG YLDLEGDFDV AVLPFSNSTN NGLLFINTTI ASIAAKEEGV SLDKREAEA WHWLQLKPGQ PMYKREAEAE AWHWLQLKPG QPMYKREADA EAWHWLQLKP GQPMYKREAD AEAWHWLQLK P GQPMY(UNK) ...String:
MRFPSIFTAV LFAASSALAA PVNTTTEDET AQIPAEAVIG YLDLEGDFDV AVLPFSNSTN NGLLFINTTI ASIAAKEEGV SLDKREAEA WHWLQLKPGQ PMYKREAEAE AWHWLQLKPG QPMYKREADA EAWHWLQLKP GQPMYKREAD AEAWHWLQLK P GQPMY(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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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

Concentration5 mg/mL
BufferpH: 7.4
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4SHEPES
100.0 mMCH3CO2KKOAc
2.5 mMMg(CH3COO)2Mg(OAc)2
1.0 mMC4H10O2S2DTT
0.02 %C56H92O25GDN
GridModel: UltrAuFoil R2/2 / Material: GOLD
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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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 recording#0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K2 QUANTUM (4k x 4k) / #0 - Detector mode: COUNTING / #0 - Number grids imaged: 1 / #0 - Average electron dose: 36.0 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K2 QUANTUM (4k x 4k) / #1 - Detector mode: COUNTING / #1 - Number grids imaged: 1 / #1 - Average electron dose: 48.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing #1

CTF correctionSoftware - Name: Gctf
Startup model#0 - Type of model: EMDB MAP
#0 - EMDB ID:

0440


#1 - Type of model: PDB ENTRY
#1 - PDB model - PDB ID:

6n3q

Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final 3D classificationSoftware - Name: RELION (ver. 3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final reconstructionAlgorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 74558
Image processing ID1
Image recording ID1
FSC plot (resolution estimation)

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Image processing #2

CTF correctionSoftware - Name: Gctf
Startup model#0 - Type of model: EMDB MAP
#0 - EMDB ID:

0440


#1 - Type of model: PDB ENTRY
#1 - PDB model - PDB ID:

6n3q

Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final 3D classificationSoftware - Name: RELION (ver. 3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final reconstructionAlgorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 15725
Image processing ID2
Image recording ID2
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6n3q

RefinementProtocol: RIGID BODY FIT
Output model

PDB-7aft:
Cryo-EM structure of the signal sequence-engaged post-translational Sec translocon

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