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- EMDB-42508: Rpn1/Nub1UBL-focused alignment of the non-substrate-engaged human... -

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Basic information

Entry
Database: EMDB / ID: EMD-42508
TitleRpn1/Nub1UBL-focused alignment of the non-substrate-engaged human 26S proteasome
Map data
Sample
  • Complex: Human 26S proteasome complexed with Nub1 and Fat 10
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 2
    • Protein or peptide: NEDD8 ultimate buster 1
    • Protein or peptide: 26S proteasome regulatory subunit 7
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 1
    • Protein or peptide: 26S proteasome regulatory subunit 4
Keywords26S Proteasome / Nub1 / Fat10 / MOTOR PROTEIN / HYDROLASE-PROTEIN BINDING complex
Function / homology
Function and homology information


regulation of ubiquitin-dependent protein catabolic process / proteasome accessory complex / proteasome regulatory particle / positive regulation of proteasomal protein catabolic process / proteasome-activating activity / proteasome regulatory particle, base subcomplex / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis ...regulation of ubiquitin-dependent protein catabolic process / proteasome accessory complex / proteasome regulatory particle / positive regulation of proteasomal protein catabolic process / proteasome-activating activity / proteasome regulatory particle, base subcomplex / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / regulation of protein catabolic process / proteasome storage granule / response to tumor necrosis factor / response to type II interferon / enzyme regulator activity / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Degradation of DVL / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Degradation of AXIN / Hh mutants are degraded by ERAD / P-body / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / Hedgehog ligand biogenesis / G2/M Checkpoints / Defective CFTR causes cystic fibrosis / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Autodegradation of the E3 ubiquitin ligase COP1 / Negative regulation of NOTCH4 signaling / Vif-mediated degradation of APOBEC3G / Regulation of RUNX3 expression and activity / Hedgehog 'on' state / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / MAPK6/MAPK4 signaling / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / ABC-family proteins mediated transport / CDK-mediated phosphorylation and removal of Cdc6 / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / Regulation of expression of SLITs and ROBOs / FCERI mediated NF-kB activation / cytoplasmic ribonucleoprotein granule / Regulation of PTEN stability and activity / Interleukin-1 signaling / Orc1 removal from chromatin / Regulation of RAS by GAPs / Regulation of RUNX2 expression and activity / osteoblast differentiation / Separation of Sister Chromatids / The role of GTSE1 in G2/M progression after G2 checkpoint / azurophil granule lumen / UCH proteinases / KEAP1-NFE2L2 pathway / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Neddylation / ER-Phagosome pathway / ubiquitin-dependent protein catabolic process / secretory granule lumen / proteasome-mediated ubiquitin-dependent protein catabolic process / ficolin-1-rich granule lumen / Ub-specific processing proteases / protein ubiquitination / ubiquitin protein ligase binding / Neutrophil degranulation / nucleolus / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / nucleus / membrane / cytosol / cytoplasm
Similarity search - Function
NEDD8 ultimate buster 1 / NEDD8 ultimate buster 1, ubiquitin-like domain / Ubiquitin-like domain / UBA/TS-N domain / : / 26S proteasome subunit RPN2, N-terminal domain / 26S proteasome regulatory complex, non-ATPase subcomplex, Rpn2/Psmd1 subunit / 26S proteasome regulatory subunit RPN2, C-terminal / 26S proteasome regulatory subunit RPN2 C-terminal domain / 26S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 subunit ...NEDD8 ultimate buster 1 / NEDD8 ultimate buster 1, ubiquitin-like domain / Ubiquitin-like domain / UBA/TS-N domain / : / 26S proteasome subunit RPN2, N-terminal domain / 26S proteasome regulatory complex, non-ATPase subcomplex, Rpn2/Psmd1 subunit / 26S proteasome regulatory subunit RPN2, C-terminal / 26S proteasome regulatory subunit RPN2 C-terminal domain / 26S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 subunit / RPN1, N-terminal / 26S proteasome non-ATPase regulatory subunit RPN1, C-terminal / RPN1 N-terminal domain / 26S proteasome non-ATPase regulatory subunit RPN1 C-terminal / : / 26S proteasome regulatory subunit 7, OB domain / Proteasome/cyclosome repeat / Proteasome/cyclosome repeat / : / Proteasomal ATPase OB C-terminal domain / Proteasomal ATPase OB C-terminal domain / HEAT repeats / Ubiquitin associated domain / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / UBA-like superfamily / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / Armadillo-like helical / Tetratricopeptide-like helical domain superfamily / Armadillo-type fold / Ubiquitin-like domain superfamily / Nucleic acid-binding, OB-fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
26S proteasome regulatory subunit 7 / 26S proteasome regulatory subunit 4 / 26S proteasome non-ATPase regulatory subunit 2 / 26S proteasome non-ATPase regulatory subunit 1 / NEDD8 ultimate buster 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.7 Å
AuthorsArkinson C / Gee CL / Martin A
Funding support United States, 1 items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Nat Struct Mol Biol / Year: 2025
Title: NUB1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome.
Authors: Connor Arkinson / Ken C Dong / Christine L Gee / Shawn M Costello / Aimee Chi Soe / Greg L Hura / Susan Marqusee / Andreas Martin /
Abstract: The ubiquitin-like modifier FAT10 targets hundreds of proteins in the mammalian immune system to the 26S proteasome for degradation. This degradation pathway requires the cofactor NUB1, yet the ...The ubiquitin-like modifier FAT10 targets hundreds of proteins in the mammalian immune system to the 26S proteasome for degradation. This degradation pathway requires the cofactor NUB1, yet the underlying mechanisms remain unknown. Here, we reconstituted a minimal in vitro system with human components and revealed that NUB1 uses the intrinsic instability of FAT10 to trap its N-terminal ubiquitin-like domain in an unfolded state and deliver it to the 26S proteasome for engagement, allowing the degradation of FAT10-ylated substrates in a ubiquitin-independent and p97-independent manner. Using hydrogen-deuterium exchange, structural modeling and site-directed mutagenesis, we identified the formation of an intricate complex with FAT10 that activates NUB1 for docking to the 26S proteasome, and our cryo-EM studies visualized the highly dynamic NUB1 complex bound to the proteasomal Rpn1 subunit during FAT10 delivery and the early stages of ATP-dependent degradation. These findings identified a previously unknown mode of cofactor-mediated, ubiquitin-independent substrate delivery to the 26S proteasome that relies on trapping partially unfolded states for engagement by the proteasomal ATPase motor.
History
DepositionOct 27, 2023-
Header (metadata) releaseNov 6, 2024-
Map releaseNov 6, 2024-
UpdateApr 23, 2025-
Current statusApr 23, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_42508.png

Downloads & links

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Map

FileDownload / File: emd_42508.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 280 pix.
= 293.44 Å		1.05 Å/pix.
x 280 pix.
= 293.44 Å		1.05 Å/pix.
x 280 pix.
= 293.44 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.048 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.64128345 - 1.2882907
Average (Standard dev.)0.00390702 (±0.024181703)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 293.44 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_42508_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_42508_half_map_2.map
Projections & Slices
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Sample components

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Entire : Human 26S proteasome complexed with Nub1 and Fat 10

EntireName: Human 26S proteasome complexed with Nub1 and Fat 10
Components
  • Complex: Human 26S proteasome complexed with Nub1 and Fat 10
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 2
    • Protein or peptide: NEDD8 ultimate buster 1
    • Protein or peptide: 26S proteasome regulatory subunit 7
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 1
    • Protein or peptide: 26S proteasome regulatory subunit 4

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Supramolecule #1: Human 26S proteasome complexed with Nub1 and Fat 10

SupramoleculeName: Human 26S proteasome complexed with Nub1 and Fat 10 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human) / Strain: HEK293
Molecular weightTheoretical: 2.6 MDa

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Macromolecule #1: 26S proteasome non-ATPase regulatory subunit 2

MacromoleculeName: 26S proteasome non-ATPase regulatory subunit 2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 100.313625 KDa
SequenceString: MEEGGRDKAP VQPQQSPAAA PGGTDEKPSG KERRDAGDKD KEQELSEEDK QLQDELEMLV ERLGEKDTSL YRPALEELRR QIRSSTTSM TSVPKPLKFL RPHYGKLKEI YENMAPGENK RFAADIISVL AMTMSGEREC LKYRLVGSQE ELASWGHEYV R HLAGEVAK ...String:
MEEGGRDKAP VQPQQSPAAA PGGTDEKPSG KERRDAGDKD KEQELSEEDK QLQDELEMLV ERLGEKDTSL YRPALEELRR QIRSSTTSM TSVPKPLKFL RPHYGKLKEI YENMAPGENK RFAADIISVL AMTMSGEREC LKYRLVGSQE ELASWGHEYV R HLAGEVAK EWQELDDAEK VQREPLLTLV KEIVPYNMAH NAEHEACDLL MEIEQVDMLE KDIDENAYAK VCLYLTSCVN YV PEPENSA LLRCALGVFR KFSRFPEALR LALMLNDMEL VEDIFTSCKD VVVQKQMAFM LGRHGVFLEL SEDVEEYEDL TEI MSNVQL NSNFLALARE LDIMEPKVPD DIYKTHLENN RFGGSGSQVD SARMNLASSF VNGFVNAAFG QDKLLTDDGN KWLY KNKDH GMLSAAASLG MILLWDVDGG LTQIDKYLYS SEDYIKSGAL LACGIVNSGV RNECDPALAL LSDYVLHNSN TMRLG SIFG LGLAYAGSNR EDVLTLLLPV MGDSKSSMEV AGVTALACGM IAVGSCNGDV TSTILQTIME KSETELKDTY ARWLPL GLG LNHLGKGEAI EAILAALEVV SEPFRSFANT LVDVCAYAGS GNVLKVQQLL HICSEHFDSK EKEEDKDKKE KKDKDKK EA PADMGAHQGV AVLGIALIAM GEEIGAEMAL RTFGHLLRYG EPTLRRAVPL ALALISVSNP RLNILDTLSK FSHDADPE V SYNSIFAMGM VGSGTNNARL AAMLRQLAQY HAKDPNNLFM VRLAQGLTHL GKGTLTLCPY HSDRQLMSQV AVAGLLTVL VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL PVSVRVGQAV DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLP VTPILEGFVI LRKNPNYDL

UniProtKB: 26S proteasome non-ATPase regulatory subunit 2

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Macromolecule #2: NEDD8 ultimate buster 1

MacromoleculeName: NEDD8 ultimate buster 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.577182 KDa
Recombinant expressionOrganism: Escherichia coli BL21 (bacteria)
SequenceString: MAQNKYLQAK LTQFLREDRI QLWKPPYTDE NKKVGLALKD LAKQYSDRLE CCENEVEKVI EEIRCKAIER GTGNDNYRTT GIATIEVFL PPRLKKDRKN LLETRLHITG RELRSKIAET FGLQENYIKI VINKKQLQLG KTLEEQGVAH NVKAMVLELK Q SEEDARKN ...String:
MAQNKYLQAK LTQFLREDRI QLWKPPYTDE NKKVGLALKD LAKQYSDRLE CCENEVEKVI EEIRCKAIER GTGNDNYRTT GIATIEVFL PPRLKKDRKN LLETRLHITG RELRSKIAET FGLQENYIKI VINKKQLQLG KTLEEQGVAH NVKAMVLELK Q SEEDARKN FQLEEEEQNE AKLKEKQIQR TKRGLEILAK RAAETVVDPE MTPYLDIANQ TGRSIRIPPS ERKALMLAMG YH EKGRAFL KRKEYGI

UniProtKB: NEDD8 ultimate buster 1

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Macromolecule #3: 26S proteasome regulatory subunit 7

MacromoleculeName: 26S proteasome regulatory subunit 7 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 48.700805 KDa
SequenceString: MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED DIQQLLKKIN ELTGIKESDT GLAPPALWDL AADKQTLQS EQPLQVARCT KIINADSEDP KYIINVKQFA KFVVDLSDQV APTDIEEGMR VGVDRNKYQI HIPLPPKIDP T VTMMQVEE ...String:
MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED DIQQLLKKIN ELTGIKESDT GLAPPALWDL AADKQTLQS EQPLQVARCT KIINADSEDP KYIINVKQFA KFVVDLSDQV APTDIEEGMR VGVDRNKYQI HIPLPPKIDP T VTMMQVEE KPDVTYSDVG GCKEQIEKLR EVVETPLLHP ERFVNLGIEP PKGVLLFGPP GTGKTLCARA VANRTDACFI RV IGSELVQ KYVGEGARMV RELFEMARTK KACLIFFDEI DAIGGARFDD GAGGDNEVQR TMLELINQLD GFDPRGNIKV LMA TNRPDT LDPALMRPGR LDRKIEFSLP DLEGRTHIFK IHARSMSVER DIRFELLARL CPNSTGAEIR SVCTEAGMFA IRAR RKIAT EKDFLEAVNK VIKSYAKFSA TPRYMTYN

UniProtKB: 26S proteasome regulatory subunit 7

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Macromolecule #4: 26S proteasome non-ATPase regulatory subunit 1

MacromoleculeName: 26S proteasome non-ATPase regulatory subunit 1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 105.958234 KDa
SequenceString: MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA ALVASKVFYH LGAFEESLNY ALGAGDLFN VNDNSEYVET IIAKCIDHYT KQCVENADLP EGEKKPIDQR LEGIVNKMFQ RCLDDHKYKQ AIGIALETRR L DVFEKTIL ...String:
MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA ALVASKVFYH LGAFEESLNY ALGAGDLFN VNDNSEYVET IIAKCIDHYT KQCVENADLP EGEKKPIDQR LEGIVNKMFQ RCLDDHKYKQ AIGIALETRR L DVFEKTIL ESNDVPGMLA YSLKLCMSLM QNKQFRNKVL RVLVKIYMNL EKPDFINVCQ CLIFLDDPQA VSDILEKLVK ED NLLMAYQ ICFDLYESAS QQFLSSVIQN LRTVGTPIAS VPGSTNTGTV PGSEKDSDSM ETEEKTSSAF VGKTPEASPE PKD QTLKMI KILSGEMAIE LHLQFLIRNN NTDLMILKNT KDAVRNSVCH TATVIANSFM HCGTTSDQFL RDNLEWLARA TNWA KFTAT ASLGVIHKGH EKEALQLMAT YLPKDTSPGS AYQEGGGLYA LGLIHANHGG DIIDYLLNQL KNASNDIVRH GGSLG LGLA AMGTARQDVY DLLKTNLYQD DAVTGEAAGL ALGLVMLGSK NAQAIEDMVG YAQETQHEKI LRGLAVGIAL VMYGRM EEA DALIESLCRD KDPILRRSGM YTVAMAYCGS GNNKAIRRLL HVAVSDVNDD VRRAAVESLG FILFRTPEQC PSVVSLL SE SYNPHVRYGA AMALGICCAG TGNKEAINLL EPMTNDPVNY VRQGALIASA LIMIQQTEIT CPKVNQFRQL YSKVINDK H DDVMAKFGAI LAQGILDAGG HNVTISLQSR TGHTHMPSVV GVLVFTQFWF WFPLSHFLSL AYTPTCVIGL NKDLKMPKV QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK KKEKEKEKKE EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQL KVLTMPETCR YQPFKPLSIG GIIILKDTSE DIEELVEPVA AHGPKIEEEE QEPEPPEPFE YIDD

UniProtKB: 26S proteasome non-ATPase regulatory subunit 1

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Macromolecule #5: 26S proteasome regulatory subunit 4

MacromoleculeName: 26S proteasome regulatory subunit 4 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 49.260504 KDa
SequenceString: MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP LVTPHTQCRL KLLKLERIKD YLLMEEEFIR NQEQMKPLE EKQEEERSKV DDLRGTPMSV GTLEEIIDDN HAIVSTSVGS EHYVSILSFV DKDLLEPGCS VLLNHKVHAV I GVLMDDTD ...String:
MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP LVTPHTQCRL KLLKLERIKD YLLMEEEFIR NQEQMKPLE EKQEEERSKV DDLRGTPMSV GTLEEIIDDN HAIVSTSVGS EHYVSILSFV DKDLLEPGCS VLLNHKVHAV I GVLMDDTD PLVTVMKVEK APQETYADIG GLDNQIQEIK ESVELPLTHP EYYEEMGIKP PKGVILYGPP GTGKTLLAKA VA NQTSATF LRVVGSELIQ KYLGDGPKLV RELFRVAEEH APSIVFIDEI DAIGTKRYDS NSGGEREIQR TMLELLNQLD GFD SRGDVK VIMATNRIET LDPALIRPGR IDRKIEFPLP DEKTKKRIFQ IHTSRMTLAD DVTLDDLIMA KDDLSGADIK AICT EAGLM ALRERRMKVT NEDFKKSKEN VLYKKQEGTP EGLYL

UniProtKB: 26S proteasome regulatory subunit 4

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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: 7.4
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.5 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
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: 2.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 373717
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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