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- EMDB-64748: Calypso/Asx/NCP-ub complex -

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Basic information

Entry
Database: EMDB / ID: EMD-64748
TitleCalypso/Asx/NCP-ub complex
Map data
Sample
  • Complex: Ternary complex of Calypso/Asx/NCP-ub
    • Protein or peptide: Histone H3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B
    • DNA: DNA (147-MER)
    • DNA: DNA (147-MER)
    • Protein or peptide: Ubiquitin carboxyl-terminal hydrolase calypso
    • Protein or peptide: Polycomb group protein Asx
    • Protein or peptide: Polyubiquitin-B
KeywordsPR-DUB / Calypso / Polycomb / TRANSCRIPTION/DNA / TRANSCRIPTION-DNA complex
Function / homology
Function and homology information


antennal development / apposition of dorsal and ventral imaginal disc-derived wing surfaces / specification of segmental identity, abdomen / sex comb development / PR-DUB complex / syncytial blastoderm mitotic cell cycle / UCH proteinases / cell fate determination / deubiquitinase activator activity / hypothalamus gonadotrophin-releasing hormone neuron development ...antennal development / apposition of dorsal and ventral imaginal disc-derived wing surfaces / specification of segmental identity, abdomen / sex comb development / PR-DUB complex / syncytial blastoderm mitotic cell cycle / UCH proteinases / cell fate determination / deubiquitinase activator activity / hypothalamus gonadotrophin-releasing hormone neuron development / anterior/posterior axis specification / female meiosis I / positive regulation of protein monoubiquitination / fat pad development / mitochondrion transport along microtubule / female gonad development / seminiferous tubule development / male meiosis I / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / energy homeostasis / neuron projection morphogenesis / regulation of proteasomal protein catabolic process / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / IRAK2 mediated activation of TAK1 complex / Prevention of phagosomal-lysosomal fusion / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Endosomal Sorting Complex Required For Transport (ESCRT) / Membrane binding and targetting of GAG proteins / Negative regulation of FLT3 / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / Constitutive Signaling by NOTCH1 HD Domain Mutants / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / APC-Cdc20 mediated degradation of Nek2A / p75NTR recruits signalling complexes / epigenetic regulation of gene expression / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Regulation of pyruvate metabolism / NF-kB is activated and signals survival / TRAF6-mediated induction of TAK1 complex within TLR4 complex / regulation of neuron apoptotic process / Pexophagy / Regulation of innate immune responses to cytosolic DNA / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / positive regulation of protein ubiquitination / animal organ morphogenesis / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Translesion synthesis by POLK / InlB-mediated entry of Listeria monocytogenes into host cell / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / Translesion synthesis by POLI / IKK complex recruitment mediated by RIP1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / regulation of mitochondrial membrane potential / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / TCF dependent signaling in response to WNT / APC/C:Cdc20 mediated degradation of Securin / Regulation of NF-kappa B signaling / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / activated TAK1 mediates p38 MAPK activation / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Regulation of signaling by CBL / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / NOTCH3 Activation and Transmission of Signal to the Nucleus / Negative regulators of DDX58/IFIH1 signaling / Assembly of the pre-replicative complex
Similarity search - Function
Polycomb protein ASX/ASX-like / Protein ASX-like, PHD domain / ASX, DEUBAD domain / Asx homology domain / PHD domain of transcriptional enhancer, Asx / UCH37-like (ULD) domain profile. / Peptidase C12, C-terminal domain / Ubiquitin carboxyl-terminal hydrolases / DEUBAD domain / DEUBAD (DEUBiquitinase ADaptor) domain profile. ...Polycomb protein ASX/ASX-like / Protein ASX-like, PHD domain / ASX, DEUBAD domain / Asx homology domain / PHD domain of transcriptional enhancer, Asx / UCH37-like (ULD) domain profile. / Peptidase C12, C-terminal domain / Ubiquitin carboxyl-terminal hydrolases / DEUBAD domain / DEUBAD (DEUBiquitinase ADaptor) domain profile. / Peptidase C12, ubiquitin carboxyl-terminal hydrolase superfamily / Ubiquitin carboxyl-terminal hydrolase, family 1 / Ubiquitin carboxyl-terminal hydrolase (UCH) catalytic domain profile. / Peptidase C12, ubiquitin carboxyl-terminal hydrolase / Papain-like cysteine peptidase superfamily / : / Histone H2A conserved site / Histone H2A signature. / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone 2A / Histone H2A / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 domain / Histone-fold / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
Histone H3 / Histone H2B / Polyubiquitin-B / Histone H4 / Histone H2A / Ubiquitin carboxyl-terminal hydrolase calypso / Polycomb group protein Asx
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly) / Xenopus laevis (African clawed frog) / Homo sapiens (human) / Escherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 5.9 Å
AuthorsWang C / He J
Funding support China, 8 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32361163669 China
National Natural Science Foundation of China (NSFC)32170189 China
National Natural Science Foundation of China (NSFC)32241021 China
Other government2023B1212060050
Other government2023B1212120009
Other government2023M743512
Other governmentGZC20232691
Other government2023A1515110923
CitationJournal: iScience / Year: 2026
Title: Structural basis of nucleosome deubiquitination by the bidentate Calypso/Asx complex.
Authors: Chi Wang / Fahui Sun / Heyu Zhao / Nan Zhang / Jiali Guan / Yuxing Zhou / Wentong Shuai / Hui Zheng / Jun He /
Abstract: The Polycomb repressive complex 1 (PRC1) and PR-DUB constitute a canonical pair of histone-modifying enzymes that deposit and remove monoubiquitinated H2A at lysine 119 (H2AK119ub1), serving as a ...The Polycomb repressive complex 1 (PRC1) and PR-DUB constitute a canonical pair of histone-modifying enzymes that deposit and remove monoubiquitinated H2A at lysine 119 (H2AK119ub1), serving as a model of dynamic epigenetic regulation. In humans, PR-DUB, composed of BAP1 and ASXL1, functions as a monomeric complex, while the homolog Calypso/Asx forms a bidentate dimer (Calypso: Asx) with an unclear chromatin engagement mechanism. Here, we present its cryo-EM structure bound to a nucleosome, revealing the molecular basis of interaction. Surprisingly, only one Calypso/Asx unit engages the nucleosome in a conformation similar to human BAP1/ASXL1, while the second remains disengaged. Structural and biochemical analysis of the positively charged Calypso C terminus suggests a "spreading" potential of the bidentate complex along chromatin, which was validated using nucleosome arrays. These findings support a model in which the bidentate Calypso/Asx complex enables processive deubiquitination along chromatin via alternating or cooperative engagement.
History
DepositionMay 21, 2025-
Header (metadata) releaseMar 18, 2026-
Map releaseMar 18, 2026-
UpdateMar 18, 2026-
Current statusMar 18, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_64748.png

Downloads & links

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Map

FileDownload / File: emd_64748.map.gz / Format: CCP4 / Size: 34.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.42 Å/pix.
x 208 pix.
= 295.36 Å		1.42 Å/pix.
x 208 pix.
= 295.36 Å		1.42 Å/pix.
x 208 pix.
= 295.36 Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.42 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0772
Minimum - Maximum-0.040015012 - 0.93524575
Average (Standard dev.)0.0034009835 (±0.023241587)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions208208208
Spacing208208208
CellA=B=C: 295.36 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_64748_msk_1.map
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Half map: #1

Fileemd_64748_half_map_1.map
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Half map: #2

Fileemd_64748_half_map_2.map
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Sample components

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Entire : Ternary complex of Calypso/Asx/NCP-ub

EntireName: Ternary complex of Calypso/Asx/NCP-ub
Components
  • Complex: Ternary complex of Calypso/Asx/NCP-ub
    • Protein or peptide: Histone H3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B
    • DNA: DNA (147-MER)
    • DNA: DNA (147-MER)
    • Protein or peptide: Ubiquitin carboxyl-terminal hydrolase calypso
    • Protein or peptide: Polycomb group protein Asx
    • Protein or peptide: Polyubiquitin-B

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Supramolecule #1: Ternary complex of Calypso/Asx/NCP-ub

SupramoleculeName: Ternary complex of Calypso/Asx/NCP-ub / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Drosophila melanogaster (fruit fly)

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Macromolecule #1: Histone H3

MacromoleculeName: Histone H3 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 15.435126 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEASEA YLVALFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3

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Macromolecule #2: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 11.394426 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG

UniProtKB: Histone H4

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Macromolecule #3: Histone H2A

MacromoleculeName: Histone H2A / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 14.297685 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGMSGRGKQG GKTRAKAKTR SSRAGLQFPV GRVHRLLRKG NYAERVGAGA PVYLAAVLEY LTAEILELAG NAARDNKKTR IIPRHLQLA VRNDEELNKL LGRVTIAQGG VLPNIQSVLL PKKTESSKSA KSK

UniProtKB: Histone H2A

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Macromolecule #4: Histone H2B

MacromoleculeName: Histone H2B / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 13.655948 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MAKSAPAPKK GSKKAVTKTQ KKDGKKRRKT RKESYAIYVY KVLKQVHPDT GISSKAMSIM NSFVNDVFER IAGEASRLAH YNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY TSAK

UniProtKB: Histone H2B

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Macromolecule #7: Ubiquitin carboxyl-terminal hydrolase calypso

MacromoleculeName: Ubiquitin carboxyl-terminal hydrolase calypso / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO / EC number: ubiquitinyl hydrolase 1
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Molecular weightTheoretical: 55.928809 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MWSHPQFEKG GGSGGGSGGG SWSHPQFEKG SSENLYFQGE FMNAAGGGSG AQAAAVAAGN NSLSHNALLS TASGATTMPM AQLADGWLE LESDPGLFTL LLKDFGCHDV QVEEVYDLQK PIESPYGFIF LFRWIEERRA RRKIVETTAE IFVKDEEAIS S IFFAQQVV ...String:
MWSHPQFEKG GGSGGGSGGG SWSHPQFEKG SSENLYFQGE FMNAAGGGSG AQAAAVAAGN NSLSHNALLS TASGATTMPM AQLADGWLE LESDPGLFTL LLKDFGCHDV QVEEVYDLQK PIESPYGFIF LFRWIEERRA RRKIVETTAE IFVKDEEAIS S IFFAQQVV PNSCATHALL SVLLNCNENN LQLGDTLSRL KTHTKGMSPE NKGLAIGNTP ELACAHNSHA MPQARRRLER TG AGVSSCR FTGEAFHFVS FVPINGQLFE LDGLKPYPMN HGGWEDSEDW TDKFRRVMAE RLGIATGEQD IRFNLMAVVP DRR IAITHK LKMLRTNQAI VSGTLQKLLK ADEQGESGNG DSQRPDTPTT LLEPSAFTAR DLQSLLKNLD TEIAINEQHL ADEN DRRHM FKVDASRRTH NYDKFICTFL SMLAHQGVLG ELVSQHLLPS KKVSGQGAAN RISKQSTTAS AGGSTAAGTA STPKT QQQQ AAAAKNGKSP SKTPGRRRKG RNKCRKRK

UniProtKB: Ubiquitin carboxyl-terminal hydrolase calypso

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Macromolecule #8: Polycomb group protein Asx

MacromoleculeName: Polycomb group protein Asx / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Molecular weightTheoretical: 37.097965 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MKTITPDTTT TTSSQHQQLL IPQADQHHQP MLQQQSLLAA PPPTMIMEHV NLVDDDEKDP LALEQLEVSP STKHTHSLRR HLPRIIVKP IPPEKKPMAP SEEAAVSTAP APPTRLICSR RIQQQQQVKA AAAAAAAAAA AAAAAAAAAQ AQATSSYPSA I SPGSKAGT ...String:
MKTITPDTTT TTSSQHQQLL IPQADQHHQP MLQQQSLLAA PPPTMIMEHV NLVDDDEKDP LALEQLEVSP STKHTHSLRR HLPRIIVKP IPPEKKPMAP SEEAAVSTAP APPTRLICSR RIQQQQQVKA AAAAAAAAAA AAAAAAAAAQ AQATSSYPSA I SPGSKAGT SQASTMREVL ASIPGFSVKP RRRSNKKLTT AAQIEQTKDG KIDLETPDSI LASTNLRALL NKQTFSLLPP LY QYNLIQL LPSVDREASE LEQPSSSASG GSPSEAIRLS ASCLNNEFFA RACLEWRERL SEGEFTPENQ LKLKTEAERE KNK LDPWKL KHFEPFWGEK NSRG

UniProtKB: Polycomb group protein Asx

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Macromolecule #9: Polyubiquitin-B

MacromoleculeName: Polyubiquitin-B / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 10.001402 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GPHHHHHHLG SHMQIFVKTL TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGC

UniProtKB: Polyubiquitin-B

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Macromolecule #5: DNA (147-MER)

MacromoleculeName: DNA (147-MER) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 45.178797 KDa
SequenceString: (DC)(DT)(DG)(DG)(DA)(DG)(DA)(DA)(DT)(DC) (DC)(DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG)(DA) (DG)(DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA) (DA)(DT)(DT)(DG)(DG)(DT)(DC)(DG)(DT)(DA) (DG) (DA)(DC)(DA)(DG)(DC)(DT) ...String:
(DC)(DT)(DG)(DG)(DA)(DG)(DA)(DA)(DT)(DC) (DC)(DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG)(DA) (DG)(DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA) (DA)(DT)(DT)(DG)(DG)(DT)(DC)(DG)(DT)(DA) (DG) (DA)(DC)(DA)(DG)(DC)(DT)(DC)(DT) (DA)(DG)(DC)(DA)(DC)(DC)(DG)(DC)(DT)(DT) (DA)(DA) (DA)(DC)(DG)(DC)(DA)(DC)(DG) (DT)(DA)(DC)(DG)(DC)(DG)(DC)(DT)(DG)(DT) (DC)(DC)(DC) (DC)(DC)(DG)(DC)(DG)(DT) (DT)(DT)(DT)(DA)(DA)(DC)(DC)(DG)(DC)(DC) (DA)(DA)(DG)(DG) (DG)(DG)(DA)(DT)(DT) (DA)(DC)(DT)(DC)(DC)(DC)(DT)(DA)(DG)(DT) (DC)(DT)(DC)(DC)(DA) (DG)(DG)(DC)(DA) (DC)(DG)(DT)(DG)(DT)(DC)(DA)(DG)(DA)(DT) (DA)(DT)(DA)(DT)(DA)(DC) (DA)(DT)(DC) (DG)(DA)(DT)(DA)

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Macromolecule #6: DNA (147-MER)

MacromoleculeName: DNA (147-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 45.57002 KDa
SequenceString: (DT)(DA)(DT)(DC)(DG)(DA)(DT)(DG)(DT)(DA) (DT)(DA)(DT)(DA)(DT)(DC)(DT)(DG)(DA)(DC) (DA)(DC)(DG)(DT)(DG)(DC)(DC)(DT)(DG) (DG)(DA)(DG)(DA)(DC)(DT)(DA)(DG)(DG)(DG) (DA) (DG)(DT)(DA)(DA)(DT)(DC) ...String:
(DT)(DA)(DT)(DC)(DG)(DA)(DT)(DG)(DT)(DA) (DT)(DA)(DT)(DA)(DT)(DC)(DT)(DG)(DA)(DC) (DA)(DC)(DG)(DT)(DG)(DC)(DC)(DT)(DG) (DG)(DA)(DG)(DA)(DC)(DT)(DA)(DG)(DG)(DG) (DA) (DG)(DT)(DA)(DA)(DT)(DC)(DC)(DC) (DC)(DT)(DT)(DG)(DG)(DC)(DG)(DG)(DT)(DT) (DA)(DA) (DA)(DA)(DC)(DG)(DC)(DG)(DG) (DG)(DG)(DG)(DA)(DC)(DA)(DG)(DC)(DG)(DC) (DG)(DT)(DA) (DC)(DG)(DT)(DG)(DC)(DG) (DT)(DT)(DT)(DA)(DA)(DG)(DC)(DG)(DG)(DT) (DG)(DC)(DT)(DA) (DG)(DA)(DG)(DC)(DT) (DG)(DT)(DC)(DT)(DA)(DC)(DG)(DA)(DC)(DC) (DA)(DA)(DT)(DT)(DG) (DA)(DG)(DC)(DG) (DG)(DC)(DC)(DT)(DC)(DG)(DG)(DC)(DA)(DC) (DC)(DG)(DG)(DG)(DA)(DT) (DT)(DC)(DT) (DC)(DC)(DA)(DG)

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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: NITROGEN

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k 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: 2.4 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6cga

Final reconstructionResolution.type: BY AUTHOR / Resolution: 5.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.2.1) / Number images used: 27764
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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