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- EMDB-45418: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome -

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Basic information

Entry
Database: EMDB / ID: EMD-45418
TitleDeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome
Map dataDeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome, fullmap
Sample
  • Complex: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome
    • Protein or peptide: Histone H3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A.1
    • Protein or peptide: Histone H2B.1
    • DNA: DNA (227-MER)
    • DNA: DNA (227-MER)
    • Protein or peptide: Chromatin-remodeling ATPase INO80
    • Protein or peptide: Ino eighty subunit 2
KeywordsChromatin Remodeler / nucleosome / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex
Function / homology
Function and homology information


sexual sporulation resulting in formation of a cellular spore / cupric reductase (NADH) activity / HATs acetylate histones / global genome nucleotide-excision repair / RNA polymerase I upstream activating factor complex / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Assembly of the ORC complex at the origin of replication / HDACs deacetylate histones ...sexual sporulation resulting in formation of a cellular spore / cupric reductase (NADH) activity / HATs acetylate histones / global genome nucleotide-excision repair / RNA polymerase I upstream activating factor complex / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Assembly of the ORC complex at the origin of replication / HDACs deacetylate histones / regulation of TOR signaling / replication fork protection complex / telomere maintenance via recombination / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / Ino80 complex / ATP-dependent chromatin remodeler activity / Oxidative Stress Induced Senescence / RMTs methylate histone arginines / postreplication repair / regulation of metabolic process / cellular response to stress / RNA Polymerase I Promoter Escape / positive regulation of transcription by RNA polymerase I / nucleolar large rRNA transcription by RNA polymerase I / Estrogen-dependent gene expression / rRNA transcription / chromosome, centromeric region / intracellular copper ion homeostasis / Ub-specific processing proteases / subtelomeric heterochromatin formation / CENP-A containing nucleosome / aerobic respiration / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / structural constituent of chromatin / nucleosome / heterochromatin formation / nucleosome assembly / chromatin organization / histone binding / transcription by RNA polymerase II / chromosome, telomeric region / chromatin remodeling / protein heterodimerization activity / DNA repair / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / ATP binding / nucleus
Similarity search - Function
DBINO domain / DNA helicase Ino80 / DNA-binding domain / DBINO domain profile. / INO80 complex subunit B-like conserved region / INO80 complex, subunit Ies2 / PAPA-1-like conserved region / PAPA-1 / : / : ...DBINO domain / DNA helicase Ino80 / DNA-binding domain / DBINO domain profile. / INO80 complex subunit B-like conserved region / INO80 complex, subunit Ies2 / PAPA-1-like conserved region / PAPA-1 / : / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / : / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H2A / Histone 2A / 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 / Helicase conserved C-terminal domain / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Histone H2B.1 / Histone H2A.1 / Ino eighty subunit 2 / Chromatin-remodeling ATPase INO80 / Histone H3 / Histone H4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Xenopus laevis (African clawed frog) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.04 Å
AuthorsWu H / Kaur U / Narlikar GJ / Cheng YF
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD) United States
CitationJournal: Science / Year: 2025
Title: Autoinhibition imposed by a large conformational switch of INO80 regulates nucleosome positioning
Authors: Kaur U / Wu H / Cheng Y / Narlikar GJ
History
DepositionJun 18, 2024-
Header (metadata) releaseJul 16, 2025-
Map releaseJul 16, 2025-
UpdateJul 16, 2025-
Current statusJul 16, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_45418.png

Downloads & links

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Map

FileDownload / File: emd_45418.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationDeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome, fullmap
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.94 Å/pix.
x 448 pix.
= 421.12 Å		0.94 Å/pix.
x 448 pix.
= 421.12 Å		0.94 Å/pix.
x 448 pix.
= 421.12 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.94 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0033
Minimum - Maximum-0.012136296 - 0.032094456
Average (Standard dev.)0.000052043037 (±0.00079523004)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions448448448
Spacing448448448
CellA=B=C: 421.12 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, The...

Fileemd_45418_additional_1.map
AnnotationDeltaNhp10 INO80 bound to S.c 0/40 nucleosome, The possible Arp8 Module Reconstruction
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, INO80 Core Module

Fileemd_45418_additional_2.map
AnnotationDeltaNhp10 INO80 bound to S.c 0/40 nucleosome, INO80 Core Module
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome,...

Fileemd_45418_half_map_1.map
AnnotationDeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome, the halfmap1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome,...

Fileemd_45418_half_map_2.map
AnnotationDeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome, the halfmap2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome

EntireName: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome
Components
  • Complex: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome
    • Protein or peptide: Histone H3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A.1
    • Protein or peptide: Histone H2B.1
    • DNA: DNA (227-MER)
    • DNA: DNA (227-MER)
    • Protein or peptide: Chromatin-remodeling ATPase INO80
    • Protein or peptide: Ino eighty subunit 2

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Supramolecule #1: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome

SupramoleculeName: DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8

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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: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 15.391007 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR EIRRFQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA IGALQESVEA YLVSLFEDTN LAAIHAKRVT IQKKDIKLAR RLRGERS

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.1

MacromoleculeName: Histone H2A.1 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 14.013177 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGGKGGKAG SAAKASQSRS AKAGLTFPVG RVHRLLRRGN YAQRIGSGAP VYLTAVLEYL AAEILELAGN AARDNKKTRI IPRHLQLAI RNDDELNKLL GNVTIAQGGV LPNIHQNLLP KKSAKATKAS QEL

UniProtKB: Histone H2A.1

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Macromolecule #4: Histone H2B.1

MacromoleculeName: Histone H2B.1 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 14.280362 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSAKAEKKPA SKAPAEKKPA AKKTSTSTDG KKRSKARKET YSSYIYKVLK QTHPDTGISQ KSMSILNSFV NDIFERIATE ASKLAAYNK KSTISAREIQ TAVRLILPGE LAKHAVSEGT RAVTKYSSST QA

UniProtKB: Histone H2B.1

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Macromolecule #7: Chromatin-remodeling ATPase INO80

MacromoleculeName: Chromatin-remodeling ATPase INO80 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 171.693812 KDa
SequenceString: MSLAVLLNKE DKDISDFSKT TAGKSAKKNS RERVADVAPT RVLDKKQAYL SQLNSEFNRI KRRDSIEQLY QDWKFINLQE FELISEWNQ QSKDWQFDNT NDSQDLHFKK LYRDMSMINK EWAEYQSFKN ANLSDIINEK DADEDEEDDE DELEDGEEDM E EDEASTGR ...String:
MSLAVLLNKE DKDISDFSKT TAGKSAKKNS RERVADVAPT RVLDKKQAYL SQLNSEFNRI KRRDSIEQLY QDWKFINLQE FELISEWNQ QSKDWQFDNT NDSQDLHFKK LYRDMSMINK EWAEYQSFKN ANLSDIINEK DADEDEEDDE DELEDGEEDM E EDEASTGR HTNGKSMRGN GIQKSRKKDA AAAAAIGKAI KDDQTHADTV VTVNGDENED GNNGEDEDND NDNENNNDND ND NENENDN DSDNDDEEEN GEEDEEEEEI EDLDEEDFAA FEEQDDNDDE DFNPDVEKRR KRSSSSSSST KLSMNSLSLI TSK KINKNI TINSDRPKIV RELIKMCNKN KHQKIKKRRF TNCIVTDYNP IDSKLNIKIT LKQYHVKRLK KLINDAKRER EREE ALKNN VGLDGNDLDN DEDGSESHKR RKLNNNTANG ADDANKRKFN TRHGLPTYGM KMNAKEARAI QRHYDNTYTT IWKDM ARKD STKMSRLVQQ IQSIRSTNFR KTSSLCAREA KKWQSKNFKQ IKDFQTRARR GIREMSNFWK KNEREERDLK KKIEKE AME QAKKEEEEKE SKRQAKKLNF LLTQTELYSH FIGRKIKTNE LEGNNVSSND SESQKNIDIS ALAPNKNDFH AIDFDNE ND EQLRLRAAEN ASNALAETRA KAKQFDDHAN AHEEEEEEDE LNFQNPTSLG EITIEQPKIL ACTLKEYQLK GLNWLANL Y DQGINGILAD EMGLGKTVQS ISVLAHLAEN HNIWGPFLVV TPASTLHNWV NEISKFLPQF KILPYWGNAN DRKVLRKFW DRKNLRYNKN APFHVMVTSY QMVVTDANYL QKMKWQYMIL DEAQAIKSSQ SSRWKNLLSF HCRNRLLLTG TPIQNSMQEL WALLHFIMP SLFDSHDEFN EWFSKDIESH AEANTKLNQQ QLRRLHMILK PFMLRRVKKN VQSELGDKIE IDVLCDLTQR Q AKLYQVLK SQISTNYDAI ENAATNDSTS NSASNSGSDQ NLINAVMQFR KVCNHPDLFE RADVDSPFSF TTFGKTTSML TA SVANNNS SVISNSNMNL SSMSSNNISN GKFTDLIYSS RNPIKYSLPR LIYEDLILPN YNNDVDIANK LKNVKFNIFN PST NYELCL FLSKLTGEPS LNEFFRVSTT PLLKRVIERT NGPKNTDSLS FKTITQELLE VTRNAPSEGV MASLLNVEKH AYER EYLNC IQRGYHPNVS APPVTIEVLG SSHVTNSINN ELFDPLISQA LSDIPAITQY NMHVKKGIPV EDFPKTGLFP EPLNK NFSS NISMPSMDRF ITESAKLRKL DELLVKLKSE GHRVLIYFQM TKMMDLMEEY LTYRQYNHIR LDGSSKLEDR RDLVHD WQT NPEIFVFLLS TRAGGLGINL TAADTVIFYD SDWNPTIDSQ AMDRAHRLGQ TRQVTVYRLL VRGTIEERMR DRAKQKE QV QQVVMEGKTQ EKNIKTIEVG ENDSEVTREG SKSISQDGIK EAASALA

UniProtKB: Chromatin-remodeling ATPase INO80

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Macromolecule #8: Ino eighty subunit 2

MacromoleculeName: Ino eighty subunit 2 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 36.210953 KDa
SequenceString: MDSEASDIEA ELSDSVSAGG EEYIDDDDYT EDIDDQIVTA KSSRRTARRS VPKGVRTSKR IRDKELSVEV DEDYDEEEDV LSPSKKRHL HTRSMDKRQV AATASEKSDI GDSKGNDGEI EDGILEEEES LEKELNRGGG KEVEKSEESY YAQNDVGQKG E EEQDGESG ...String:
MDSEASDIEA ELSDSVSAGG EEYIDDDDYT EDIDDQIVTA KSSRRTARRS VPKGVRTSKR IRDKELSVEV DEDYDEEEDV LSPSKKRHL HTRSMDKRQV AATASEKSDI GDSKGNDGEI EDGILEEEES LEKELNRGGG KEVEKSEESY YAQNDVGQKG E EEQDGESG GYEDNEPSIS KESDELVSVV NGNGNEEDDE VEATKENTTD STRSTTTRSK MLLDLLEDGG SKKKLTDEEI QL RRAENAR KRKNLSEKRL EEEKQDTINK LLKKRAGKSR SHLPNDDEKN DGSSSFVKPR RPYNSEGMTR ILRRYEEDLF CTF

UniProtKB: Ino eighty subunit 2

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Macromolecule #5: DNA (227-MER)

MacromoleculeName: DNA (227-MER) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 70.34775 KDa
SequenceString: (DT)(DC)(DG)(DG)(DT)(DA)(DC)(DC)(DC)(DG) (DG)(DG)(DG)(DA)(DT)(DC)(DC)(DT)(DC)(DT) (DA)(DG)(DA)(DG)(DT)(DG)(DG)(DG)(DA) (DG)(DC)(DT)(DC)(DG)(DG)(DA)(DA)(DC)(DA) (DC) (DT)(DA)(DT)(DC)(DC)(DG) ...String:
(DT)(DC)(DG)(DG)(DT)(DA)(DC)(DC)(DC)(DG) (DG)(DG)(DG)(DA)(DT)(DC)(DC)(DT)(DC)(DT) (DA)(DG)(DA)(DG)(DT)(DG)(DG)(DG)(DA) (DG)(DC)(DT)(DC)(DG)(DG)(DA)(DA)(DC)(DA) (DC) (DT)(DA)(DT)(DC)(DC)(DG)(DA)(DC) (DT)(DG)(DG)(DC)(DA)(DC)(DC)(DG)(DG)(DC) (DA)(DA) (DG)(DG)(DT)(DC)(DG)(DC)(DT) (DG)(DT)(DT)(DC)(DA)(DA)(DT)(DA)(DC)(DA) (DT)(DG)(DC) (DA)(DC)(DA)(DG)(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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Macromolecule #6: DNA (227-MER)

MacromoleculeName: DNA (227-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 69.840398 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) (DC)(DT)(DG)(DT)(DG)(DC)(DA)(DT)(DG)(DT) (DA)(DT)(DT)(DG)(DA)(DA)(DC) (DA)(DG) (DC)(DG)(DA)(DC)(DC)(DT)(DT)(DG)(DC)(DC) (DG)(DG)(DT)(DG)(DC)(DC)(DA)(DG) (DT) (DC)(DG)(DG)(DA)(DT)(DA)(DG)(DT)(DG)(DT) (DT)(DC)(DC)(DG)(DA)(DG)(DC)(DT)(DC) (DC)(DC)(DA)(DC)(DT)(DC)(DT)(DA)(DG)(DA) (DG)(DG)(DA)(DT)(DC)(DC)(DC)(DC)(DG)(DG) (DG)(DT)(DA)(DC)(DC)(DG)(DA)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statecell

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: OTHER

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 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: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.04 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 40107
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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