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- EMDB-8680: Conformational Landscape of the p28-Bound Human Proteasome Regula... -

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Entry
Database: EMDB / ID: EMD-8680
TitleConformational Landscape of the p28-Bound Human Proteasome Regulatory Particle
Map dataFinal Map of Rpn1-p28-AAA subcomplex in the TA4 state, corrected with a B-factor of -400
Sample
  • Complex: Proteasome regulatory particle
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 10
    • Protein or peptide: 26S proteasome regulatory subunit 7
    • Protein or peptide: 26S proteasome regulatory subunit 4
    • Protein or peptide: 26S proteasome regulatory subunit 6B
    • Protein or peptide: 26S proteasome regulatory subunit 10B
    • Protein or peptide: 26S proteasome regulatory subunit 6A
    • Protein or peptide: 26S proteasome regulatory subunit 8
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 2
Keywordsp28 / 26S proteasome / regulatory particle / 19S / gankyrin / HYDROLASE
Function / homology
Function and homology information


cytoplasmic sequestering of NF-kappaB / positive regulation of inclusion body assembly / proteasome regulatory particle assembly / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / proteasome accessory complex / positive regulation of proteasomal protein catabolic process / proteasome regulatory particle / cytosolic proteasome complex / proteasome-activating activity ...cytoplasmic sequestering of NF-kappaB / positive regulation of inclusion body assembly / proteasome regulatory particle assembly / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / proteasome accessory complex / positive regulation of proteasomal protein catabolic process / proteasome regulatory particle / cytosolic proteasome complex / proteasome-activating activity / proteasome regulatory particle, base subcomplex / negative regulation of programmed cell death / Regulation of ornithine decarboxylase (ODC) / intermediate filament cytoskeleton / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / negative regulation of MAPK cascade / negative regulation of NF-kappaB transcription factor activity / regulation of protein catabolic process / negative regulation of release of cytochrome c from mitochondria / proteasome storage granule / negative regulation of DNA damage response, signal transduction by p53 class mediator / blastocyst development / transcription factor binding / positive regulation of cyclin-dependent protein serine/threonine kinase activity / general transcription initiation factor binding / positive regulation of RNA polymerase II transcription preinitiation complex assembly / enzyme regulator activity / inclusion body / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / : / cytoskeletal protein binding / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / positive regulation of protein ubiquitination / Asymmetric localization of PCP proteins / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Degradation of DVL / TNFR2 non-canonical NF-kB pathway / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / protein localization to plasma membrane / P-body / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Degradation of GLI1 by the proteasome / Degradation of AXIN / Defective CFTR causes cystic fibrosis / Activation of NF-kappaB in B cells / Negative regulation of NOTCH4 signaling / Hedgehog ligand biogenesis / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Vif-mediated degradation of APOBEC3G / G2/M Checkpoints / Hedgehog 'on' state / Autodegradation of the E3 ubiquitin ligase COP1 / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / Regulation of RUNX3 expression and activity / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / MAPK6/MAPK4 signaling / Degradation of beta-catenin by the destruction complex / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / ABC-family proteins mediated transport / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / CDK-mediated phosphorylation and removal of Cdc6 / CLEC7A (Dectin-1) signaling / osteoblast differentiation / SCF(Skp2)-mediated degradation of p27/p21 / Regulation of expression of SLITs and ROBOs / cytoplasmic ribonucleoprotein granule / FCERI mediated NF-kB activation / Interleukin-1 signaling / Regulation of PTEN stability and activity / Orc1 removal from chromatin / Regulation of RAS by GAPs / Separation of Sister Chromatids / Regulation of RUNX2 expression and activity / UCH proteinases / The role of GTSE1 in G2/M progression after G2 checkpoint / KEAP1-NFE2L2 pathway / protein-macromolecule adaptor activity / Antigen processing: Ubiquitination & Proteasome degradation / Downstream TCR signaling / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Neddylation / RUNX1 regulates transcription of genes involved in differentiation of HSCs / ubiquitin-dependent protein catabolic process / ER-Phagosome pathway / cytoplasmic vesicle / positive regulation of cell growth / proteasome-mediated ubiquitin-dependent protein catabolic process
Similarity search - Function
: / 26S proteasome regulatory subunit 7, OB 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 / Proteasome/cyclosome repeat / Proteasome/cyclosome repeat / Proteasomal ATPase OB C-terminal domain ...: / 26S proteasome regulatory subunit 7, OB 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 / Proteasome/cyclosome repeat / Proteasome/cyclosome repeat / Proteasomal ATPase OB C-terminal domain / Proteasomal ATPase OB C-terminal domain / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / Ankyrin repeat / Ankyrin repeats (3 copies) / ATPase family associated with various cellular activities (AAA) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / ATPase, AAA-type, core / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Armadillo-like helical / Armadillo-type fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Nucleic acid-binding, OB-fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
26S proteasome non-ATPase regulatory subunit 10 / 26S proteasome regulatory subunit 6A / 26S proteasome regulatory subunit 7 / 26S proteasome regulatory subunit 6B / 26S proteasome regulatory subunit 4 / 26S proteasome regulatory subunit 8 / 26S proteasome regulatory subunit 10B / 26S proteasome non-ATPase regulatory subunit 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 8.3 Å
AuthorsLu Y / Wu J
CitationJournal: Mol Cell / Year: 2017
Title: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle.
Authors: Ying Lu / Jiayi Wu / Yuanchen Dong / Shuobing Chen / Shuangwu Sun / Yong-Bei Ma / Qi Ouyang / Daniel Finley / Marc W Kirschner / Youdong Mao /
Abstract: The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of ...The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly.
History
DepositionApr 13, 2017-
Header (metadata) releaseAug 23, 2017-
Map releaseAug 23, 2017-
UpdateMar 13, 2024-
Current statusMar 13, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
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  • Atomic models: PDB-5vho
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

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Map

FileDownload / File: emd_8680.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFinal Map of Rpn1-p28-AAA subcomplex in the TA4 state, corrected with a B-factor of -400
Voxel sizeX=Y=Z: 0.86 Å
Density
Contour LevelBy AUTHOR: 0.004 / Movie #1: 0.004
Minimum - Maximum-0.005733738 - 0.011247279
Average (Standard dev.)-0.0001463491 (±0.0007843967)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 309.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.860.860.86
M x/y/z360360360
origin x/y/z0.0000.0000.000
length x/y/z309.600309.600309.600
α/β/γ90.00090.00090.000
start NX/NY/NZ-34-26-36
NX/NY/NZ528549
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS360360360
D min/max/mean-0.0060.011-0.000

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Supplemental data

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Sample components

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Entire : Proteasome regulatory particle

EntireName: Proteasome regulatory particle
Components
  • Complex: Proteasome regulatory particle
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 10
    • Protein or peptide: 26S proteasome regulatory subunit 7
    • Protein or peptide: 26S proteasome regulatory subunit 4
    • Protein or peptide: 26S proteasome regulatory subunit 6B
    • Protein or peptide: 26S proteasome regulatory subunit 10B
    • Protein or peptide: 26S proteasome regulatory subunit 6A
    • Protein or peptide: 26S proteasome regulatory subunit 8
    • Protein or peptide: 26S proteasome non-ATPase regulatory subunit 2

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Supramolecule #1: Proteasome regulatory particle

SupramoleculeName: Proteasome regulatory particle / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: 26S proteasome non-ATPase regulatory subunit 10

MacromoleculeName: 26S proteasome non-ATPase regulatory subunit 10 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.14249 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: CVSNLMVCNL AYSGKLEELK ESILADKSLA TRTDQDSRTA LHWACSAGHT EIVEFLLQLG VPVNDKDDAG WSPLHIAASA GRDEIVKAL LGKGAQVNAV NQNGCTPLHY AASKNRHEIA VMLLEGGANP DAKDHYEATA MHRAAAKGNL KMIHILLYYK A STNIQDTE ...String:
CVSNLMVCNL AYSGKLEELK ESILADKSLA TRTDQDSRTA LHWACSAGHT EIVEFLLQLG VPVNDKDDAG WSPLHIAASA GRDEIVKAL LGKGAQVNAV NQNGCTPLHY AASKNRHEIA VMLLEGGANP DAKDHYEATA MHRAAAKGNL KMIHILLYYK A STNIQDTE GNTPLHLACD EERVEEAKLL VSQGASIYIE NKEEKTPLQV AKGGLGLILK RMVEG

UniProtKB: 26S proteasome non-ATPase regulatory subunit 10

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Macromolecule #2: 26S proteasome regulatory subunit 7

MacromoleculeName: 26S proteasome regulatory subunit 7 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.861551 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: DPTVTMMQVE EKPDVTYSDV GGCKEQIEKL REVVETPLLH PERFVNLGIE PPKGVLLFGP PGTGKTLCAR AVANRTDACF IRVIGSELV QKYVGEGARM VRELFEMART KKACLIFFDE IDAIGGARFD DGAGGDNEVQ RTMLELINQL DGFDPRGNIK V LMATNRPD ...String:
DPTVTMMQVE EKPDVTYSDV GGCKEQIEKL REVVETPLLH PERFVNLGIE PPKGVLLFGP PGTGKTLCAR AVANRTDACF IRVIGSELV QKYVGEGARM VRELFEMART KKACLIFFDE IDAIGGARFD DGAGGDNEVQ RTMLELINQL DGFDPRGNIK V LMATNRPD TLDPALMRPG RLDRKIEFSL PDLEGRTHIF KIHARSMSVE RDIRFELLAR LCPNSTGAEI RSVCTEAGMF AI RARRKIA TEKDFLEAVN KVIKSYAKFS

UniProtKB: 26S proteasome regulatory subunit 7

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Macromolecule #3: 26S proteasome regulatory subunit 4

MacromoleculeName: 26S proteasome regulatory subunit 4 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.958395 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: TDPLVTVMKV EKAPQETYAD IGGLDNQIQE IKESVELPLT HPEYYEEMGI KPPKGVILYG PPGTGKTLLA KAVANQTSAT FLRVVGSEL IQKYLGDGPK LVRELFRVAE EHAPSIVFID EIDAIGTKRY DSNSGGEREI QRTMLELLNQ LDGFDSRGDV K VIMATNRI ...String:
TDPLVTVMKV EKAPQETYAD IGGLDNQIQE IKESVELPLT HPEYYEEMGI KPPKGVILYG PPGTGKTLLA KAVANQTSAT FLRVVGSEL IQKYLGDGPK LVRELFRVAE EHAPSIVFID EIDAIGTKRY DSNSGGEREI QRTMLELLNQ LDGFDSRGDV K VIMATNRI ETLDPALIRP GRIDRKIEFP LPDEKTKKRI FQIHTSRMTL ADDVTLDDLI MAKDDLSGAD IKAICTEAGL MA LRERRMK VTNEDFKKSK ENVLYKKQEG

UniProtKB: 26S proteasome regulatory subunit 4

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Macromolecule #4: 26S proteasome regulatory subunit 6B

MacromoleculeName: 26S proteasome regulatory subunit 6B / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.497975 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: PEADSSIMML TSDQKPDVMY ADIGGMDIQK QEVREAVELP LTHFELYKQI GIDPPRGVLM YGPPGCGKTM LAKAVAHHTT AAFIRVVGS EFVQKYLGEG PRMVRDVFRL AKENAPAIIF IDEIDAIATK RFDAQTGADR EVQRILLELL NQMDGFDQNV N VKVIMATN ...String:
PEADSSIMML TSDQKPDVMY ADIGGMDIQK QEVREAVELP LTHFELYKQI GIDPPRGVLM YGPPGCGKTM LAKAVAHHTT AAFIRVVGS EFVQKYLGEG PRMVRDVFRL AKENAPAIIF IDEIDAIATK RFDAQTGADR EVQRILLELL NQMDGFDQNV N VKVIMATN RADTLDPALL RPGRLDRKIE FPLPDRRQKR LIFSTITSKM NLSEEVDLED YVARPDKISG ADINSICQES GM LAVRENR YIVLAKDFEK AYKTV

UniProtKB: 26S proteasome regulatory subunit 6B

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Macromolecule #5: 26S proteasome regulatory subunit 10B

MacromoleculeName: 26S proteasome regulatory subunit 10B / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.434889 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: GNVSYSEIGG LSEQIRELRE VIELPLTNPE LFQRVGIIPP KGCLLYGPPG TGKTLLARAV ASQLDCNFLK VVSSSIVDKY IGESARLIR EMFNYARDHQ PCIIFMDEID AIGGRRFSEG TSADREIQRT LMELLNQMDG FDTLHRVKMI MATNRPDTLD P ALLRPGRL ...String:
GNVSYSEIGG LSEQIRELRE VIELPLTNPE LFQRVGIIPP KGCLLYGPPG TGKTLLARAV ASQLDCNFLK VVSSSIVDKY IGESARLIR EMFNYARDHQ PCIIFMDEID AIGGRRFSEG TSADREIQRT LMELLNQMDG FDTLHRVKMI MATNRPDTLD P ALLRPGRL DRKIHIDLPN EQARLDILKI HAGPITKHGE IDYEAIVKLS DGFNGADLRN VCTEAGMFAI RADHDFVVQE DF MKAVRKV ADSKKLESKL DYKPV

UniProtKB: 26S proteasome regulatory subunit 10B

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Macromolecule #6: 26S proteasome regulatory subunit 6A

MacromoleculeName: 26S proteasome regulatory subunit 6A / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.773246 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: TEYDSRVKAM EVDERPTEQY SDIGGLDKQI QELVEAIVLP MNHKEKFENL GIQPPKGVLM YGPPGTGKTL LARACAAQTK ATFLKLAGP QLVQMFIGDG AKLVRDAFAL AKEKAPSIIF IDELDAIGTK RFDSEKAGDR EVQRTMLELL NQLDGFQPNT Q VKVIAATN ...String:
TEYDSRVKAM EVDERPTEQY SDIGGLDKQI QELVEAIVLP MNHKEKFENL GIQPPKGVLM YGPPGTGKTL LARACAAQTK ATFLKLAGP QLVQMFIGDG AKLVRDAFAL AKEKAPSIIF IDELDAIGTK RFDSEKAGDR EVQRTMLELL NQLDGFQPNT Q VKVIAATN RVDILDPALL RSGRLDRKIE FPMPNEEARA RIMQIHSRKM NVSPDVNYEE LARCTDDFNG AQCKAVCVEA GM IALRRGA TELTHEDYME GILEVQAKKK

UniProtKB: 26S proteasome regulatory subunit 6A

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Macromolecule #7: 26S proteasome regulatory subunit 8

MacromoleculeName: 26S proteasome regulatory subunit 8 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.501363 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: KVDPLVSLMM VEKVPDSTYE MIGGLDKQIK EIKEVIELPV KHPELFEALG IAQPKGVLLY GPPGTGKTLL ARAVAHHTDC TFIRVSGSE LVQKFIGEGA RMVRELFVMA REHAPSIIFM DEIDSIGSSR LEGGSGGDSE VQRTMLELLN QLDGFEATKN I KVIMATNR ...String:
KVDPLVSLMM VEKVPDSTYE MIGGLDKQIK EIKEVIELPV KHPELFEALG IAQPKGVLLY GPPGTGKTLL ARAVAHHTDC TFIRVSGSE LVQKFIGEGA RMVRELFVMA REHAPSIIFM DEIDSIGSSR LEGGSGGDSE VQRTMLELLN QLDGFEATKN I KVIMATNR IDILDSALLR PGRIDRKIEF PPPNEEARLD ILKIHSRKMN LTRGINLRKI AELMPGASGA EVKGVCTEAG MY ALRERRV HVTQEDFEMA VAKVMQKDS

UniProtKB: 26S proteasome regulatory subunit 8

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Macromolecule #8: 26S proteasome non-ATPase regulatory subunit 2

MacromoleculeName: 26S proteasome non-ATPase regulatory subunit 2 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 93.790188 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: RDKAPVQPQQ SPAAAPGGTD EKPSGKERRD AGDKDKEQEL SEEDKQLQDE LEMLVERLGE KDTSLYRPAL EELRRQIRSS TTSMTSVPK PLKFLRPHYG KLKEIYENMA PGENKRFAAD IISVLAMTMS GERECLKYRL VGSQEELASW GHEYVRHLAG E VAKEWQEL ...String:
RDKAPVQPQQ SPAAAPGGTD EKPSGKERRD AGDKDKEQEL SEEDKQLQDE LEMLVERLGE KDTSLYRPAL EELRRQIRSS TTSMTSVPK PLKFLRPHYG KLKEIYENMA PGENKRFAAD IISVLAMTMS GERECLKYRL VGSQEELASW GHEYVRHLAG E VAKEWQEL DDAEKVQREP LLTLVKEIVP YNMAHNAEHE ACDLLMEIEQ VDMLEKDIDE NAYAKVCLYL TSCVNYVPEP EN SALLRCA LGVFRKFSRF PEALRLALML NDMELVEDIF TSCKDVVVQK QMAFMLGRHG VFLELSEDVE EYEDLTEIMS NVQ LNSNFL ALARELDIME PKVPDDIYKT HLENNRFGGS GSQVDSARMN LASSFVNGFV NAAFGQDKLL TDDGNKWLYK NKDH GMLSA AASLGMILLW DVDGGLTQID KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG SIFGL GLAY AGSNREDVLT LLLPVMGDSK SSMEVAGVTA LACGMIAVGS CNGDVTSTIL QTIMEKSETE LKDTYARWLP LGLGLN HLG KGEAIEAILA ALEVVSEPFR SFANTLVDVC AYAGSGNVLK VQQLLHICSE HFDSKEKEED KDKKEKKDKD KKEAPAD MG AHQGVAVLGI ALIAMGEEIG AEMALRTFGH LLRYGEPTLR RAVPLALALI SVSNPRLNIL DTLSKFSHDA DPEVSYNS I FAMGMVGSGT NNARLAAMLR QLAQYHAKDP NNLFMVRLAQ GLTHLGKGTL TLCPYHSDRQ LMSQVAVAGL LTVLVSFLD VRNIILGKSH YVLYGLVAAM QPRMLVTFDE ELRPLPVSVR VGQAVDVV

UniProtKB: 26S proteasome non-ATPase regulatory subunit 2

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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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TECNAI ARCTICA
Electron beamAcceleration voltage: 200 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: 50.0 e/Å2
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: PROJECTION MATCHING
Final reconstructionResolution.type: BY AUTHOR / Resolution: 8.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 9004

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