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- EMDB-54399: State 3 MAP 1 SETD2 bound to distal H3 of upstream nucleosome -

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Basic information

Entry
Database: EMDB / ID: EMD-54399
TitleState 3 MAP 1 SETD2 bound to distal H3 of upstream nucleosome
Map data
Sample
  • Complex: State 3 SETD2 bound to distal H3 tail
    • DNA: Non-template DNA
    • Protein or peptide: Histone-lysine N-methyltransferase SETD2
    • DNA: Template DNA
    • Protein or peptide: Histone H3.2
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A type 1-B/E
    • Protein or peptide: Histone H2B type 1-K
    • Protein or peptide: FACT complex subunit SPT16
KeywordsRNA Pol II Activated elongation complex Co-transcriptional H3K36me3 SETD2 / TRANSCRIPTION
Function / homology
Function and homology information


peptidyl-lysine trimethylation / FACT complex / microtubule cytoskeleton organization involved in mitosis / [histone H3]-lysine36 N-trimethyltransferase / regulation of mRNA export from nucleus / histone H3K36 trimethyltransferase activity / histone H3K36 methyltransferase activity / response to alkaloid / nucleosome organization / response to type I interferon ...peptidyl-lysine trimethylation / FACT complex / microtubule cytoskeleton organization involved in mitosis / [histone H3]-lysine36 N-trimethyltransferase / regulation of mRNA export from nucleus / histone H3K36 trimethyltransferase activity / histone H3K36 methyltransferase activity / response to alkaloid / nucleosome organization / response to type I interferon / protein-lysine N-methyltransferase activity / positive regulation of ossification / regulation of protein localization to chromatin / nucleosome disassembly / response to metal ion / positive regulation of DNA-templated transcription, elongation / histone H3 methyltransferase activity / regulation of double-strand break repair via homologous recombination / endodermal cell differentiation / positive regulation of interferon-alpha production / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / alpha-tubulin binding / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / mismatch repair / negative regulation of megakaryocyte differentiation / Formation of HIV elongation complex in the absence of HIV Tat / protein localization to CENP-A containing chromatin / nucleosome binding / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / RNA Polymerase II Transcription Elongation / CENP-A containing nucleosome / Formation of RNA Pol II elongation complex / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / RNA Polymerase II Pre-transcription Events / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Deposition of new CENPA-containing nucleosomes at the centromere / positive regulation of autophagy / telomere organization / Inhibition of DNA recombination at telomere / Interleukin-7 signaling / RNA Polymerase I Promoter Opening / Meiotic synapsis / Assembly of the ORC complex at the origin of replication / Transferases; Transferring one-carbon groups; Methyltransferases / SUMOylation of chromatin organization proteins / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / DNA methylation / Condensation of Prophase Chromosomes / Chromatin modifications during the maternal to zygotic transition (MZT) / SIRT1 negatively regulates rRNA expression / HCMV Late Events / innate immune response in mucosa / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / regulation of cytokinesis / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / HDMs demethylate histones / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / HDACs deacetylate histones / stem cell differentiation / TP53 Regulates Transcription of DNA Repair Genes / Nonhomologous End-Joining (NHEJ) / transcription elongation by RNA polymerase II / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / G2/M DNA damage checkpoint / Metalloprotease DUBs / NoRC negatively regulates rRNA expression / DNA Damage/Telomere Stress Induced Senescence / B-WICH complex positively regulates rRNA expression / PKMTs methylate histone lysines / Meiotic recombination / Pre-NOTCH Transcription and Translation / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / Transcriptional regulation of granulopoiesis / UCH proteinases / HCMV Early Events / antimicrobial humoral immune response mediated by antimicrobial peptide / structural constituent of chromatin / antibacterial humoral response / E3 ubiquitin ligases ubiquitinate target proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / nucleosome / heterochromatin formation / RUNX1 regulates transcription of genes involved in differentiation of HSCs / nucleosome assembly / Processing of DNA double-strand break ends
Similarity search - Function
FACT complex subunit Spt16, peptidase M24-like domain / : / FACT complex subunit SPT16, C-terminal domain / : / FACT complex subunit SPT16 PH-like domain / FACT complex subunit Spt16 domain / FACT complex subunit (SPT16/CDC68) / FACT complex subunit (SPT16/CDC68) / FACT complex subunit Spt16, N-terminal lobe domain / FACT complex subunit Spt16 ...FACT complex subunit Spt16, peptidase M24-like domain / : / FACT complex subunit SPT16, C-terminal domain / : / FACT complex subunit SPT16 PH-like domain / FACT complex subunit Spt16 domain / FACT complex subunit (SPT16/CDC68) / FACT complex subunit (SPT16/CDC68) / FACT complex subunit Spt16, N-terminal lobe domain / FACT complex subunit Spt16 / FACT complex subunit SPT16 N-terminal lobe domain / FACT complex subunit SPT16 N-terminal lobe domain / Histone-lysine N-methyltransferase SETD2, animal / Set2 Rpb1 interacting domain superfamily / SETD2/Set2, SET domain / Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain / Histone chaperone Rttp106-like, middle domain / Histone chaperone Rttp106-like / Set2 Rpb1 interacting domain / SRI (Set2 Rpb1 interacting) domain / AWS domain / AWS domain / AWS domain profile. / associated with SET domains / Creatinase/Aminopeptidase P/Spt16, N-terminal / Cysteine-rich motif following a subset of SET domains / Post-SET domain / Post-SET domain profile. / TFIIS/LEDGF domain superfamily / Peptidase M24 / Metallopeptidase family M24 / Creatinase/aminopeptidase-like / WW domain / WW/rsp5/WWP domain signature. / SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / SET domain / WW domain / SET domain superfamily / SET domain profile. / SET domain / : / Histone H2B signature. / Histone H2A conserved site / Histone H2A 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 / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / PH-like domain superfamily
Similarity search - Domain/homology
Histone H2B type 1-K / Histone H2A type 1-B/E / Histone H4 / Histone H3.2 / Histone-lysine N-methyltransferase SETD2 / FACT complex subunit SPT16
Similarity search - Component
Biological speciesHomo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.66 Å
AuthorsWalshe JL / Ochmann M / Dienemann C / Cramer P
Funding support Germany, 1 items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: To Be Published
Title: Molecular mechanism of co-transcriptional H3K36 methylation by SETD2
Authors: Walshe JL / Ochmann M / Neef U / Dybkov O / Dienemann C / Oberthuer C / Zheenbekova A / Urlaub H / Cramer P
History
DepositionJul 15, 2025-
Header (metadata) releaseSep 24, 2025-
Map releaseSep 24, 2025-
UpdateSep 24, 2025-
Current statusSep 24, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_54399.png

Downloads & links

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Map

FileDownload / File: emd_54399.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 300 pix.
= 315. Å		1.05 Å/pix.
x 300 pix.
= 315. Å		1.05 Å/pix.
x 300 pix.
= 315. Å

Surface

Projections

Slices (1/3)

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.05 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.011
Minimum - Maximum-0.032902334 - 0.06314203
Average (Standard dev.)0.0001602928 (±0.0016742715)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 315.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_54399_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_54399_half_map_2.map
Projections & Slices
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Histogram

Histogram (log scale)

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Sample components

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Entire : State 3 SETD2 bound to distal H3 tail

EntireName: State 3 SETD2 bound to distal H3 tail
Components
  • Complex: State 3 SETD2 bound to distal H3 tail
    • DNA: Non-template DNA
    • Protein or peptide: Histone-lysine N-methyltransferase SETD2
    • DNA: Template DNA
    • Protein or peptide: Histone H3.2
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A type 1-B/E
    • Protein or peptide: Histone H2B type 1-K
    • Protein or peptide: FACT complex subunit SPT16

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Supramolecule #1: State 3 SETD2 bound to distal H3 tail

SupramoleculeName: State 3 SETD2 bound to distal H3 tail / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Non-template DNA

MacromoleculeName: Non-template DNA / type: dna / ID: 1 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 61.155906 KDa
SequenceString: (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) ...String:
(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)(DG) (DA)(DT)(DA)(DT)(DC)(DG)(DA)(DT)(DC)(DA) (DC)(DT)(DG)(DT)(DC)(DG)(DC) (DG)(DG) (DC)(DC)(DC)(DT)(DT)(DG)(DT)(DG)(DT)(DT) (DC)(DA)(DG)(DG)(DA)(DG)(DC)(DC) (DA) (DG)(DC)(DA)(DG)(DG)(DG)(DA)(DG)(DC)(DT) (DG)(DG)(DG)(DA)(DG)(DC)

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Macromolecule #3: Template DNA

MacromoleculeName: Template DNA / type: dna / ID: 3 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 60.52248 KDa
SequenceString: (DG)(DC)(DT)(DC)(DC)(DC)(DA)(DG)(DC)(DT) (DC)(DC)(DC)(DT)(DG)(DC)(DT)(DG)(DG)(DC) (DT)(DC)(DC)(DG)(DA)(DG)(DT)(DG)(DG) (DG)(DT)(DT)(DC)(DT)(DG)(DC)(DC)(DG)(DC) (DG) (DA)(DC)(DA)(DG)(DT)(DG) ...String:
(DG)(DC)(DT)(DC)(DC)(DC)(DA)(DG)(DC)(DT) (DC)(DC)(DC)(DT)(DG)(DC)(DT)(DG)(DG)(DC) (DT)(DC)(DC)(DG)(DA)(DG)(DT)(DG)(DG) (DG)(DT)(DT)(DC)(DT)(DG)(DC)(DC)(DG)(DC) (DG) (DA)(DC)(DA)(DG)(DT)(DG)(DA)(DT) (DC)(DG)(DA)(DT)(DA)(DT)(DC)(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)

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Macromolecule #2: Histone-lysine N-methyltransferase SETD2

MacromoleculeName: Histone-lysine N-methyltransferase SETD2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: [histone H3]-lysine36 N-trimethyltransferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 127.887328 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: SNAETSVPPG SALVGPSCVM DDFRDPQRWK ECAKQGKMPC YFDLIEENVY LTERKKNKSH RDIKRMQCEC TPLSKDERAQ GEIACGEDC LNRLLMIECS SRCPNGDYCS NRRFQRKQHA DVEVILTEKK GWGLRAAKDL PSNTFVLEYC GEVLDHKEFK A RVKEYARN ...String:
SNAETSVPPG SALVGPSCVM DDFRDPQRWK ECAKQGKMPC YFDLIEENVY LTERKKNKSH RDIKRMQCEC TPLSKDERAQ GEIACGEDC LNRLLMIECS SRCPNGDYCS NRRFQRKQHA DVEVILTEKK GWGLRAAKDL PSNTFVLEYC GEVLDHKEFK A RVKEYARN KNIHYYFMAL KNDEIIDATQ KGNCSRFMNH SCEPNCETQK WTVNGQLRVG FFTTKLVPSG SELTFDYQFQ RY GKEAQKC FCGSANCRGY LGGENRVSIR AAGGKMKKER SRKKDSVDGE LEALMENGEG LSDKNQVLSL SRLMVRIETL EQK LTCLEL IQNTHSQSCL KSFLERHGLS LLWIWMAELG DGRESNQKLQ EEIIKTLEHL PIPTKNMLEE SKVLPIIQRW SQTK TAVPP LSEGDGYSSE NTSRAHTPLN TPDPSTKLST EADTDTPKKL MFRRLKIISE NSMDSAISDA TSELEGKDGK EDLDQ LENV PVEEEEELQS QQLLPQQLPE CKVDSETNIE ASKLPTSEPE ADAEIELKES NGTKLEEPIN EETPSQDEEE GVSDVE SER SQEQPDKTVD ISDLATKLLD SWKDLKEVYR IPKKSQTEKE NTTTERGRDA VGFRDQTPAP KTPNRSRERD PDKQTQN KE KRKRRSSLSP PSSAYERGTK RPDDRYDTPT SKKKVRIKDR NKLSTEERRK LFEQEVAQRE AQKQQQQMQN LGMTSPLP Y DSLGYNAPHH PFAGYPPGYP MQAYVDPSNP NAGKVLLPTP SMDPVCSPAP YDHAQPLVGH STEPLSAPPP VPVVPHVAA PVEVSSSQYV AQSDGVVHQD SSVAVLPVPA PGPVQGQNYS VWDSNQQSVS VQQQYSPAQS QATIYYQGQT CPTVYGVTSP YSQTTPPIV QSYAQPSLQY IQGQQIFTAH PQGVVVQPAA AVTTIVAPGQ PQPLQPSEMV VTNNLLDLPP PSPPKPKTIV L PPNWKTAR DPEGKIYYYH VITRQTQWDP PTWESPGDDA SLEHEAEMDL GTPTYDENPM KASKKPKTAE ADTSSELAKK SK EVFRKEM SQFIVQCLNP YRKPDCKVGR ITTTEDFKHL ARKLTHGVMN KELKYCKNPE DLECNENVKH KTKEYIKKYM QKF GAVYKP KEDTELE

UniProtKB: Histone-lysine N-methyltransferase SETD2

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Macromolecule #4: Histone H3.2

MacromoleculeName: Histone H3.2 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.391052 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVMKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEASEA YLVGLFEDTN LAAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3.2

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Macromolecule #5: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
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 #6: Histone H2A type 1-B/E

MacromoleculeName: Histone H2A type 1-B/E / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.721133 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SNAPWMSGRG KQGGKARAKA KTRSSRAGLQ FPVGRVHRLL RKGNYSERVG AGAPVYLAAV LEYLTAEILE LAGNAARDNK KTRIIPRHL QLAIRNDEEL NKLLGRVTIA QGGVLPNIQA VLLPKKTESH HKAKGK

UniProtKB: Histone H2A type 1-B/E

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Macromolecule #7: Histone H2B type 1-K

MacromoleculeName: Histone H2B type 1-K / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.921213 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSAK

UniProtKB: Histone H2B type 1-K

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Macromolecule #8: FACT complex subunit SPT16

MacromoleculeName: FACT complex subunit SPT16 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 120.290961 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: SNMAVTLDKD AYYRRVKRLY SNWRKGEDEY ANVDAIVVSV GVDEEIVYAK STALQTWLFG YELTDTIMVF CDDKIIFMAS KKKVEFLKQ IANTKGNENA NGAPAITLLI REKNESNKSS FDKMIEAIKE SKNGKKIGVF SKDKFPGEFM KSWNDCLNKE G FDKIDISA ...String:
SNMAVTLDKD AYYRRVKRLY SNWRKGEDEY ANVDAIVVSV GVDEEIVYAK STALQTWLFG YELTDTIMVF CDDKIIFMAS KKKVEFLKQ IANTKGNENA NGAPAITLLI REKNESNKSS FDKMIEAIKE SKNGKKIGVF SKDKFPGEFM KSWNDCLNKE G FDKIDISA VVAYTIAVKE DGELNLMKKA ASITSEVFNK FFKERVMEIV DADEKVRHSK LAESVEKAIE EKKYLAGADP ST VEMCYPP IIQSGGNYNL KFSVVSDKNH MHFGAITCAM GIRFKSYCSN LVRTLMVDPS QEVQENYNFL LQLQEELLKE LRH GVKICD VYNAVMDVVK KQKPELLNKI TKNLGFGMGI EFREGSLVIN SKNQYKLKKG MVFSINLGFS DLTNKEGKKP EEKT YALFI GDTVLVDEDG PATVLTSVKK KVKNVGIFLK NEDEEEEEEE KDEAEDLLGR GSRAALLTER TRNEMTAEEK RRAHQ KELA AQLNEEAKRR LTEQKGEQQI QKARKSNVSY KNPSLMPKEP HIREMKIYID KKYETVIMPV FGIATPFHIA TIKNIS MSV EGDYTYLRIN FYCPGSALGR NEGNIFPNPE ATFVKEITYR ASNIKAPGEQ TVPALNLQNA FRIIKEVQKR YKTREAE EK EKEGIVKQDS LVINLNRSNP KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL YNNIKHALFQ PCDGEMII V LHFHLKNAIM FGKKRHTDVQ FYTEVGEITT DLGKHQHMHD RDDLYAEQME REMRHKLKTA FKNFIEKVEA LTKEELEFE VPFRDLGFNG APYRSTCLLQ PTSSALVNAT EWPPFVVTLD EVELIHFERV QFHLKNFDMV IVYKDYSKKV TMINAIPVAS LDPIKEWLN SCDLKYTEGV QSLNWTKIMK TIVDDPEGFF EQGGWSFLEP EGEGSDAEEG DSESEIEDET FNPSEDDYEE E EEDSDEDY SSEAEESDYS KESLGSEEES GKDWDELEEE ARKADRESRY EEEEEQSRSM SRKRKASVHS SGRGSNRGSR HS SAPPKKK RK

UniProtKB: FACT complex subunit SPT16

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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

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 39.83 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 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: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.66 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 17088
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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