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- EMDB-62690: The cryo-EM structure of ATRX in complex with the nucleosome in t... -

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Basic information

Entry
Database: EMDB / ID: EMD-62690
TitleThe cryo-EM structure of ATRX in complex with the nucleosome in the ADP.BeFx-bound state (composite)
Map datacomposite map
Sample
  • Complex: ATRX C-terminal domains in complex with the nucleosome
    • Protein or peptide: Histone H3.3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A type 1-C
    • Protein or peptide: Histone H2B type 1-C/E/F/G/I
    • Protein or peptide: Histone H4
    • DNA: DNA (207-MER)
    • DNA: DNA (207-MER)
    • Protein or peptide: Transcriptional regulator ATRX
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
Keywordschromatin remodeler / nucleosome / DNA BINDING PROTEIN
Function / homology
Function and homology information


post-embryonic forelimb morphogenesis / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / positive regulation of nuclear cell cycle DNA replication / chromosome, subtelomeric region / Sertoli cell development / Barr body / chromosome organization involved in meiotic cell cycle / chromo shadow domain binding ...post-embryonic forelimb morphogenesis / Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations / Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / positive regulation of nuclear cell cycle DNA replication / chromosome, subtelomeric region / Sertoli cell development / Barr body / chromosome organization involved in meiotic cell cycle / chromo shadow domain binding / meiotic spindle organization / DNA translocase activity / negative regulation of chromosome condensation / cellular response to hydroxyurea / condensed chromosome, centromeric region / pericentric heterochromatin formation / inner kinetochore / muscle cell differentiation / oocyte maturation / histone H3K9me2/3 reader activity / protein localization to chromosome, telomeric region / nucleosomal DNA binding / nucleus organization / seminiferous tubule development / nuclear chromosome / forebrain development / positive regulation of telomere maintenance / replication fork processing / spermatid development / single fertilization / subtelomeric heterochromatin formation / RNA polymerase II core promoter sequence-specific DNA binding / pericentric heterochromatin / negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / heterochromatin / Packaging Of Telomere Ends / embryo implantation / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere / telomere organization / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / RNA Polymerase I Promoter Opening / Inhibition of DNA recombination at telomere / Assembly of the ORC complex at the origin of replication / Meiotic synapsis / SUMOylation of chromatin organization proteins / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / DNA helicase activity / DNA methylation / Condensation of Prophase Chromosomes / Chromatin modifications during the maternal to zygotic transition (MZT) / SIRT1 negatively regulates rRNA expression / HCMV Late Events / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / innate immune response in mucosa / Defective pyroptosis / DNA damage response, signal transduction by p53 class mediator / HDACs deacetylate histones / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / RNA Polymerase I Promoter Escape / Nonhomologous End-Joining (NHEJ) / Transcriptional regulation by small RNAs / HDMs demethylate histones / Formation of the beta-catenin:TCF transactivating complex / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / chromatin DNA binding / PML body / NoRC negatively regulates rRNA expression / Negative Regulation of CDH1 Gene Transcription / G2/M DNA damage checkpoint / PKMTs methylate histone lysines / B-WICH complex positively regulates rRNA expression / DNA Damage/Telomere Stress Induced Senescence / male gonad development / Meiotic recombination / Pre-NOTCH Transcription and Translation / multicellular organism growth / Activation of anterior HOX genes in hindbrain development during early embryogenesis / Transcriptional regulation of granulopoiesis / Metalloprotease DUBs / RMTs methylate histone arginines / HCMV Early Events / osteoblast differentiation / structural constituent of chromatin / UCH proteinases / nucleosome / antimicrobial humoral immune response mediated by antimicrobial peptide / nucleosome assembly / heterochromatin formation / HATs acetylate histones / antibacterial humoral response / E3 ubiquitin ligases ubiquitinate target proteins
Similarity search - Function
ATRX, ADD domain / : / : / Cysteine Rich ADD domain / ATRX C-terminal domain / ADD domain / ADD domain profile. / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal ...ATRX, ADD domain / : / : / Cysteine Rich ADD domain / ATRX C-terminal domain / ADD domain / ADD domain profile. / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / : / 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 / Zinc finger, FYVE/PHD-type / 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 domain / 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 / Zinc finger, RING/FYVE/PHD-type / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Transcriptional regulator ATRX / Histone H4 / Histone H2B type 1-C/E/F/G/I / Histone H3.3 / Histone H2A type 1-C
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsZhou K / Duan S / Liu Y
Funding support Hong Kong, 1 items
OrganizationGrant numberCountry
The University Grants Committee, Research Grants Council (RGC)27122123 Hong Kong
CitationJournal: To Be Published
Title: Mechanistic insights into chromatin modulation by the orphan remodeler ATRX
Authors: Zhou K / Liu Y
History
DepositionDec 11, 2024-
Header (metadata) releaseJun 17, 2026-
Map releaseJun 17, 2026-
UpdateJun 17, 2026-
Current statusJun 17, 2026Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_62690.png

Downloads & links

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Map

FileDownload / File: emd_62690.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationcomposite map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.96 Å/pix.
x 384 pix.
= 366.989 Å		0.96 Å/pix.
x 384 pix.
= 366.989 Å		0.96 Å/pix.
x 384 pix.
= 366.989 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.9557 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.18
Minimum - Maximum-0.9329963 - 1.6188864
Average (Standard dev.)0.0038108625 (±0.028118497)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 366.9888 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: consensus map

Fileemd_62690_additional_1.map
Annotationconsensus map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : ATRX C-terminal domains in complex with the nucleosome

EntireName: ATRX C-terminal domains in complex with the nucleosome
Components
  • Complex: ATRX C-terminal domains in complex with the nucleosome
    • Protein or peptide: Histone H3.3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A type 1-C
    • Protein or peptide: Histone H2B type 1-C/E/F/G/I
    • Protein or peptide: Histone H4
    • DNA: DNA (207-MER)
    • DNA: DNA (207-MER)
    • Protein or peptide: Transcriptional regulator ATRX
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: ATRX C-terminal domains in complex with the nucleosome

SupramoleculeName: ATRX C-terminal domains in complex with the nucleosome
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 320 KDa

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Macromolecule #1: Histone H3.3

MacromoleculeName: Histone H3.3 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.360983 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSAA IGALQEASEA YLVGLFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3.3

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Macromolecule #2: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 10.004796 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
AKRHRKVLRD NIQGITKPAI RRLARRGGVK RISGLIYEET RGVLKVFLEN VIRDAVTYTE HAKRKTVTAM DVVYALKRQG RTLYGFG

UniProtKB: Histone H4

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Macromolecule #3: Histone H2A type 1-C

MacromoleculeName: Histone H2A type 1-C / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.135523 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIR NDEELNKLLG RVTIAQGGVL PNIQAVLLPK KTESHHKAKG K

UniProtKB: Histone H2A type 1-C

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Macromolecule #4: Histone H2B type 1-C/E/F/G/I

MacromoleculeName: Histone H2B type 1-C/E/F/G/I / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.937213 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSSK

UniProtKB: Histone H2B type 1-C/E/F/G/I

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Macromolecule #5: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.86159 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
RHRKVLRDNI QGITKPAIRR LARRGGVKRI SGLIYEETRG VLKVFLENVI RDAVTYTEHA KRKTVTAMDV VYALKRQGRT LYGFGG

UniProtKB: Histone H4

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Macromolecule #8: Transcriptional regulator ATRX

MacromoleculeName: Transcriptional regulator ATRX / type: protein_or_peptide / ID: 8
Details: 1901-1989 UNK (Poly-A to represent the backbone) "HHHHHHHHHHDYKDDDDK" is expression tag
Number of copies: 1 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 143.105172 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: SKSVPVTVDD DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK KRTGKQNEEN PGDEEAKNQV NSESDSDSEE SKKPRYRHR LLRHKLTVSD GESGEEKKTK PKEHKEVKGR NRRKVSSEDS EDSDFQESGV SEEVSESEDE QRPRTRSAKK A ELEENQRS ...String:
SKSVPVTVDD DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK KRTGKQNEEN PGDEEAKNQV NSESDSDSEE SKKPRYRHR LLRHKLTVSD GESGEEKKTK PKEHKEVKGR NRRKVSSEDS EDSDFQESGV SEEVSESEDE QRPRTRSAKK A ELEENQRS YKQKKKRRRI KVQEDSSSEN KSNSEEEEEE KEEEEEEEEE EEEEEEDEND DSKSPGKGRK KIRKILKDDK LR TETQNAL KEEEERRKRI AEREREREKL REVIEIEDAS PTKCPITTKL VLDEDEETKE PLVQVHRNMV IKLKPHQVDG VQF MWDCCC ESVKKTKKSP GSGCILAHCM GLGKTLQVVS FLHTVLLCDK LDFSTALVVC PLNTALNWMN EFEKWQEGLK DDEK LEVSE LATVKRPQER SYMLQRWQED GGVMIIGYEM YRNLAQGRNV KSRKLKEIFN KALVDPGPDF VVCDEGHILK NEASA VSKA MNSIRSRRRI ILTGTPLQNN LIEYHCMVNF IKENLLGSIK EFRNRFINPI QNGQCADSTM VDVRVMKKRA HILYEM LAG CVQRKDYTAL TKFLPPKHEY VLAVRMTSIQ CKLYQYYLDH LTGVGNNSEG GRGKAGAKLF QDFQMLSRIW THPWCLQ LD YISKENKG(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)(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)SSSNPSSP APDWYKDFVT DADAEVL EH SGKMVLLFEI LRMAEEIGDK VLVFSQSLIS LDLIEDFLEL ASREKTEDKD KPLIYKGEGK WLRNIDYYRL DGSTTAQS R KKWAEEFNDE TNVRGRLFII STKAGSLGIN LVAANRVIIF DASWNPSYDI QSIFRVYRFG QTKPVYVYRF LAQGTMEDK IYDRQVTKQS LSFRVVDQQQ VERHFTMNEL TELYTFEPDL LDDPNSEKKK KRDTPMLPKD TILAELLQIH KEHIVGYHEH DSLLDHKEE EELTEEERKA AWAEYEAEKK GLTMRFNIPT GTNLPPVSFN SQTPYIPFNL GALSAMSNQQ LEDLINQGRE K VVEATNSV TAVRIQPLED IISAVWKENM NLSEAQVQAL ALSRQASQEL DVKRREAIYN DVLTKQQMLI SCVQRILMNR RL QQQYNQQ QQQQMTYQQA TLGHLMMPKP PNLIMNPSNY QQIDMRGMYQ PVAGGMQPPP LQRAPPPMRS KNPGPSQGKS MHH HHHHHH HHDYKDDDDK

UniProtKB: Transcriptional regulator ATRX

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Macromolecule #6: DNA (207-MER)

MacromoleculeName: DNA (207-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 63.673582 KDa
SequenceString: (DA)(DT)(DC)(DT)(DA)(DA)(DT)(DA)(DC)(DT) (DA)(DG)(DG)(DA)(DC)(DC)(DC)(DT)(DA)(DT) (DA)(DC)(DG)(DC)(DG)(DG)(DC)(DC)(DG) (DC)(DA)(DT)(DC)(DG)(DG)(DA)(DG)(DA)(DA) (DT) (DC)(DC)(DC)(DG)(DG)(DT) ...String:
(DA)(DT)(DC)(DT)(DA)(DA)(DT)(DA)(DC)(DT) (DA)(DG)(DG)(DA)(DC)(DC)(DC)(DT)(DA)(DT) (DA)(DC)(DG)(DC)(DG)(DG)(DC)(DC)(DG) (DC)(DA)(DT)(DC)(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)(DT)(DG)(DC) (DA) (DT)(DG)(DT)(DG)(DG)(DA)(DT)(DC)(DC)(DG) (DA)(DA)(DT)(DT)(DC)(DA)(DT)(DA)(DT) (DT)(DA)(DA)(DT)(DG)(DA)(DT)

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Macromolecule #7: DNA (207-MER)

MacromoleculeName: DNA (207-MER) / type: dna / ID: 7 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 64.144879 KDa
SequenceString: (DA)(DT)(DC)(DA)(DT)(DT)(DA)(DA)(DT)(DA) (DT)(DG)(DA)(DA)(DT)(DT)(DC)(DG)(DG)(DA) (DT)(DC)(DC)(DA)(DC)(DA)(DT)(DG)(DC) (DA)(DA)(DT)(DC)(DG)(DA)(DT)(DG)(DT)(DA) (DT) (DA)(DT)(DA)(DT)(DC)(DT) ...String:
(DA)(DT)(DC)(DA)(DT)(DT)(DA)(DA)(DT)(DA) (DT)(DG)(DA)(DA)(DT)(DT)(DC)(DG)(DG)(DA) (DT)(DC)(DC)(DA)(DC)(DA)(DT)(DG)(DC) (DA)(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)(DG)(DA)(DT)(DG)(DC)(DG) (DG) (DC)(DC)(DG)(DC)(DG)(DT)(DA)(DT)(DA)(DG) (DG)(DG)(DT)(DC)(DC)(DT)(DA)(DG)(DT) (DA)(DT)(DT)(DA)(DG)(DA)(DT)

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Macromolecule #9: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 1 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #10: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 10 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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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

Concentration1.50 mg/mL
BufferpH: 7.8
GridModel: UltrAuFoil / Material: GOLD / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 90 sec.
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 147422
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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