EMDB-13004: Pol II-CSB-CSA-DDB1-UVSSA (Structure1)

Basic information

• Entry: Database: EMDB / ID: EMD-13004
• Title: Pol II-CSB-CSA-DDB1-UVSSA (Structure1)
• Map data: Main map.

Sample

• Complex: RNA polymerase II elongation complex with CSB, CSA-DDB1 and UVSSA.
  • Complex: DNA directed RNA polymerase
    • Protein or peptide: x 12 types
  • Complex: NTS, TS & RNA
    • DNA: x 2 types
    • RNA: x 1 types
  • Complex: DNA Repair proteins, CSB element and scaffold protein
    • Protein or peptide: x 5 types
• Ligand: x 2 types

• Keywords: transcription / DNA repair

Function / homology

Function:

RNA polymerase inhibitor activity / negative regulation of double-strand break repair via nonhomologous end joining / regulation of transcription-coupled nucleotide-excision repair / nucleotide-excision repair complex / : / response to auditory stimulus / DNA protection / transcription elongation factor complex / regulation of transcription elongation by RNA polymerase II / B-WICH complex positively regulates rRNA expression / RNA Polymerase I Transcription Initiation / RNA Polymerase I Promoter Escape / RNA Polymerase I Transcription Termination / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Polymerase III Transcription Initiation From Type 3 Promoter / Formation of RNA Pol II elongation complex / Formation of the Early Elongation Complex / Transcriptional regulation by small RNAs / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / FGFR2 alternative splicing / RNA polymerase II transcribes snRNA genes / mRNA Capping / mRNA Splicing - Minor Pathway / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Elongation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Pol II CTD phosphorylation and interaction with CE / Estrogen-dependent gene expression / mRNA Splicing - Major Pathway / mRNA Polyadenylation / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / double-strand break repair via classical nonhomologous end joining / single strand break repair / RNA polymerase binding / positive regulation of DNA-templated transcription, elongation / positive regulation by virus of viral protein levels in host cell / spindle assembly involved in female meiosis / chromatin-protein adaptor activity / epigenetic programming in the zygotic pronuclei / ATP-dependent chromatin remodeler activity / UV-damage excision repair / ATP-dependent DNA damage sensor activity / biological process involved in interaction with symbiont / regulation of mitotic cytokinesis / regulation of mitotic cell cycle phase transition / regulation of miRNA-mediated gene silencing / regulation of natural killer cell activation / WD40-repeat domain binding / regulation of cell cycle phase transition / Cul4A-RING E3 ubiquitin ligase complex / Cul4-RING E3 ubiquitin ligase complex / regulation of stem cell population maintenance / positive regulation of transcription by RNA polymerase III / positive regulation of transcription by RNA polymerase I / organelle membrane / Cul4B-RING E3 ubiquitin ligase complex / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / RNA polymerase II complex binding / RNA Polymerase I Transcription Initiation / ubiquitin ligase complex scaffold activity / response to UV / negative regulation of adipose tissue development / regulation of cellular response to stress / viral release from host cell / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / positive regulation of translational initiation / cullin family protein binding / protein tyrosine kinase activator activity / ATP-dependent activity, acting on DNA / neurogenesis / regulation of DNA-templated DNA replication initiation / positive regulation of viral genome replication / positive regulation of gluconeogenesis / protein autoubiquitination / termination of RNA polymerase III transcription / positive regulation of double-strand break repair via homologous recombination / transcription initiation at RNA polymerase III promoter / ubiquitin-like ligase-substrate adaptor activity / DNA damage checkpoint signaling / RNA polymerase I complex / RNA polymerase III complex / RNA polymerase II, core complex / transcription elongation by RNA polymerase I / tRNA transcription by RNA polymerase III / protein localization to chromatin / transcription by RNA polymerase I / transcription-coupled nucleotide-excision repair / translation initiation factor binding / regulation of embryonic development / positive regulation of DNA repair / replication fork processing / positive regulation of RNA splicing / DNA-templated transcription elongation

Domain/homology:

: / UV-stimulated scaffold protein A / : / : / Uncharacterized conserved protein (DUF2043) / UVSSA N-terminal domain / Zinc finger UVSSA-type profile. / : / Rad26/CSB winged helix DNA-binding domain / DNA excision repair protein Rad28/ERCC8/Ckn1/ATCSA-1 / : / RNA-binding domain, S1 / ENTH/VHS / : / RSE1/DDB1/CPSF1 second beta-propeller / Cleavage/polyadenylation specificity factor, A subunit, C-terminal / Cleavage/polyadenylation specificity factor, A subunit, N-terminal / : / CPSF A subunit region / RSE1/DDB1/CPSF1 first beta-propeller / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / DNA-directed RNA polymerase II subunit Rpb4-like / RNA polymerase Rpb4/RPC9, core / DNA-directed RNA-polymerase II subunit / RNA polymerase Rpb1 C-terminal repeat / RNA polymerase II, heptapeptide repeat, eukaryotic / Eukaryotic RNA polymerase II heptapeptide repeat. / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 7 superfamily / RNA polymerase Rpb1, domain 7 / Rpb4/RPC9 superfamily / Pol II subunit B9, C-terminal zinc ribbon / RNA polymerase RBP11 / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / Zinc finger TFIIS-type signature. / RNA polymerase Rpb7-like , N-terminal / RNA polymerase Rpb7-like, N-terminal domain superfamily / RNA polymerase subunit Rpb7-like / SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397 / HRDC-like superfamily / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / DNA-directed RNA polymerase, M/15kDa subunit / RNA polymerases M/15 Kd subunit / RNA polymerase subunit 9 / DNA-directed RNA polymerase M, 15kDa subunit, conserved site / RNA polymerases M / 15 Kd subunits signature. / DNA-directed RNA polymerase subunit/transcription factor S / RNA polymerase, Rpb8 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / RNA polymerase Rpb8 / RNA polymerase subunit 8 / RNA polymerase, Rpb5, N-terminal / RNA polymerase Rpb5, N-terminal domain superfamily / RNA polymerase Rpb5, N-terminal domain / : / DNA-directed RNA polymerase, subunit RPB6 / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerase subunit RPB10 / RNA polymerases N / 8 kDa subunit / RNA polymerases N / 8 Kd subunits signature. / RNA polymerase, subunit H/Rpb5, conserved site / RNA polymerases H / 23 Kd subunits signature. / DNA directed RNA polymerase, 7 kDa subunit / Zinc finger, TFIIS-type / RNA polymerase archaeal subunit P/eukaryotic subunit RPABC4 / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / RNA polymerase subunit CX / DNA-directed RNA polymerase, 30-40kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo3/Rpb3/RPAC1 / RNA polymerases D / 30 to 40 Kd subunits signature. / DNA-directed RNA polymerase Rpb11, 13-16kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo11 / RNA polymerases L / 13 to 16 Kd subunits signature. / RNA polymerase subunit RPABC4/transcription elongation factor Spt4 / DNA-directed RNA polymerase, RBP11-like dimerisation domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerase, subunit H/Rpb5 C-terminal / DNA-directed RNA polymerase subunit Rpo5/Rpb5 / RPB5-like RNA polymerase subunit superfamily / RNA polymerase Rpb5, C-terminal domain / Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit / DNA-directed RNA polymerase, 14-18kDa subunit, conserved site / RNA polymerases K / 14 to 18 Kd subunits signature. / Ribosomal protein S1-like RNA-binding domain / S1 RNA binding domain / S1 domain / DNA-directed RNA polymerase, subunit beta-prime / Helicase conserved C-terminal domain

Component:

DNA-directed RNA polymerase II subunit RPB4 / DNA-directed RNA polymerase RBP11-like dimerisation domain-containing protein / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase II subunit RPB7 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerase II subunit RPB1 / DNA-directed RNA polymerase II subunit RPB9 / DNA excision repair protein ERCC-6 / DNA excision repair protein ERCC-8 / DNA damage-binding protein 1 / UV-stimulated scaffold protein A

• Biological species: Sus scrofa (pig) / Homo sapiens (human)
• Method: single particle reconstruction / cryo EM / Resolution: 2.8 Å
• Authors: Kokic G / Cramer P

Funding support

Germany, 2 items

Organization	Grant number	Country
German Research Foundation (DFG)	EXC 2067/1 39072994, SFB860, SPP2191	Germany
European Research Council (ERC)	882357	Germany

• Citation: Journal: Nature / Year: 2021; Title: Structural basis of human transcription-DNA repair coupling.; Authors: Goran Kokic / Felix R Wagner / Aleksandar Chernev / Henning Urlaub / Patrick Cramer / ; Abstract: Transcription-coupled DNA repair removes bulky DNA lesions from the genome and protects cells against ultraviolet (UV) irradiation. Transcription-coupled DNA repair begins when RNA polymerase II (Pol II) stalls at a DNA lesion and recruits the Cockayne syndrome protein CSB, the E3 ubiquitin ligase, CRL4 and UV-stimulated scaffold protein A (UVSSA). Here we provide five high-resolution structures of Pol II transcription complexes containing human transcription-coupled DNA repair factors and the elongation factors PAF1 complex (PAF) and SPT6. Together with biochemical and published data, the structures provide a model for transcription-repair coupling. Stalling of Pol II at a DNA lesion triggers replacement of the elongation factor DSIF by CSB, which binds to PAF and moves upstream DNA to SPT6. The resulting elongation complex, EC, uses the CSA-stimulated translocase activity of CSB to pull on upstream DNA and push Pol II forward. If the lesion cannot be bypassed, CRL4 spans over the Pol II clamp and ubiquitylates the RPB1 residue K1268, enabling recruitment of TFIIH to UVSSA and DNA repair. Conformational changes in CRL4 lead to ubiquitylation of CSB and to release of transcription-coupled DNA repair factors before transcription may continue over repaired DNA.

History

Deposition	May 26, 2021	-
Header (metadata) release	Oct 6, 2021	-
Map release	Oct 6, 2021	-
Update	Jul 9, 2025	-
Current status	Jul 9, 2025	Processing site: PDBe / Status: Released

Map

• File: Download / File: emd_13004.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Annotation: Main map.
• Voxel size: X=Y=Z: 1.05 Å

Density

Contour Level	By AUTHOR: 0.01 / Movie #1: 0.01
Minimum - Maximum	-0.10523341 - 0.18084967
Average (Standard dev.)	-0.0004728839 (±0.0031010401)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 400 400 400 Spacing 400 400 400
Cell	A=B=C: 419.99997 Å α=β=γ: 90.0 °

CCP4 map header:

mode	Image stored as Reals
Å/pix. X/Y/Z	1.05	1.05	1.05
M x/y/z	400	400	400
origin x/y/z	0.000	0.000	0.000
length x/y/z	420.000	420.000	420.000
α/β/γ	90.000	90.000	90.000
start NX/NY/NZ	29	29	0
NX/NY/NZ	140	137	200
MAP C/R/S	1	2	3
start NC/NR/NS	0	0	0
NC/NR/NS	400	400	400
D min/max/mean	-0.105	0.181	-0.000

Supplemental data

Mask #1

• File: emd_13004_msk_1.map

Mask #2

• File: emd_13004_msk_2.map

Mask #3

• File: emd_13004_msk_3.map

Mask #4

• File: emd_13004_msk_4.map

Mask #5

• File: emd_13004_msk_5.map

Additional map: Half map corresponding to the map focused refined on CSA-UVSSA.

• File: emd_13004_additional_1.map
• Annotation: Half map corresponding to the map focused refined on CSA-UVSSA.

Additional map: Half map corresponding to the map focused refined on CSA-UVSSA.

• File: emd_13004_additional_10.map
• Annotation: Half map corresponding to the map focused refined on CSA-UVSSA.

Additional map: Half map corresponding to the map focused refined on CSB.

• File: emd_13004_additional_2.map
• Annotation: Half map corresponding to the map focused refined on CSB.

Additional map: Half map corresponding to the map focused refined on CSA-DDB1.

• File: emd_13004_additional_3.map
• Annotation: Half map corresponding to the map focused refined on CSA-DDB1.

Additional map: Half map corresponding to the map focused refined on CSB.

• File: emd_13004_additional_4.map
• Annotation: Half map corresponding to the map focused refined on CSB.

Additional map: Half map corresponding to the map focused refined on CSA-DDB1.

• File: emd_13004_additional_5.map
• Annotation: Half map corresponding to the map focused refined on CSA-DDB1.

Additional map: Half map corresponding to the map focused refined on DDB1.

• File: emd_13004_additional_6.map
• Annotation: Half map corresponding to the map focused refined on DDB1.

Additional map: Half map corresponding to the map focused refined on DDB1.

• File: emd_13004_additional_7.map
• Annotation: Half map corresponding to the map focused refined on DDB1.

Additional map: Half map corresponding to the map focused refined on Pol II.

• File: emd_13004_additional_8.map
• Annotation: Half map corresponding to the map focused refined on Pol II.

Additional map: Half map corresponding to the map focused refined on Pol II.

• File: emd_13004_additional_9.map
• Annotation: Half map corresponding to the map focused refined on Pol II.

Half map: Half map corresponding to the main map.

• File: emd_13004_half_map_1.map
• Annotation: Half map corresponding to the main map.

Half map: Half map corresponding to the main map.

• File: emd_13004_half_map_2.map
• Annotation: Half map corresponding to the main map.

Sample components

Entire : RNA polymerase II elongation complex with CSB, CSA-DDB1 and UVSSA.

• Entire: Name: RNA polymerase II elongation complex with CSB, CSA-DDB1 and UVSSA.

Components

• Complex: RNA polymerase II elongation complex with CSB, CSA-DDB1 and UVSSA.
  • Complex: DNA directed RNA polymerase
    • Protein or peptide: DNA-directed RNA polymerase II subunit RPB1
    • Protein or peptide: DNA-directed RNA polymerase subunit beta
    • Protein or peptide: DNA-directed RNA polymerase II subunit RPB3
    • Protein or peptide: RPOL4c domain-containing protein
    • Protein or peptide: DNA-directed RNA polymerase II subunit E
    • Protein or peptide: DNA-directed RNA polymerase II subunit F
    • Protein or peptide: DNA-directed RNA polymerase II subunit RPB7
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3
    • Protein or peptide: DNA-directed RNA polymerase II subunit RPB9
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5
    • Protein or peptide: RNA_pol_L_2 domain-containing protein
    • Protein or peptide: RNA polymerase II subunit K
  • Complex: NTS, TS & RNA
    • DNA: NTS
    • DNA: TS
    • RNA: RNA
  • Complex: DNA Repair proteins, CSB element and scaffold protein
    • Protein or peptide: DNA excision repair protein ERCC-8
    • Protein or peptide: DNA excision repair protein ERCC-6
    • Protein or peptide: CSB element
    • Protein or peptide: UV-stimulated scaffold protein A
    • Protein or peptide: DNA damage-binding protein 1
• Ligand: ZINC ION
• Ligand: MAGNESIUM ION

Supramolecule #1: RNA polymerase II elongation complex with CSB, CSA-DDB1 and UVSSA.

• Supramolecule: Name: RNA polymerase II elongation complex with CSB, CSA-DDB1 and UVSSA.; type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#20

Supramolecule #2: DNA directed RNA polymerase

• Supramolecule: Name: DNA directed RNA polymerase / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#12
• Source (natural): Organism: Sus scrofa (pig)

Supramolecule #3: NTS, TS & RNA

• Supramolecule: Name: NTS, TS & RNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #13-#15
• Source (natural): Organism: Homo sapiens (human) / Synthetically produced: Yes

Supramolecule #4: DNA Repair proteins, CSB element and scaffold protein

• Supramolecule: Name: DNA Repair proteins, CSB element and scaffold protein / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #16-#20
• Source (natural): Organism: Homo sapiens (human)

Macromolecule #1: DNA-directed RNA polymerase II subunit RPB1

• Macromolecule: Name: DNA-directed RNA polymerase II subunit RPB1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 217.450078 KDa

Sequence

String:

MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIE LAKPVFHVGF LVKTMKVLRC VCFFCSKLLV DSNNPKIKDI LAKSKGQPKK RLTHVYDLCK GKNICEGGEE M DNKFGVEQ PEGDEDLTKE KGHGGCGRYQ PRIRRSGLEL YAEWKHVNED SQEKKILLSP ERVHEIFKRI SDEECFVLGM EP RYARPEW MIVTVLPVPP LSVRPAVVMQ GSARNQDDLT HKLADIVKIN NQLRRNEQNG AAAHVIAEDV KLLQFHVATM VDN ELPGLP RAMQKSGRPL KSLKQRLKGK EGRVRGNLMG KRVDFSARTV ITPDPNLSID QVGVPRSIAA NMTFAEIVTP FNID RLQEL VRRGNSQYPG AKYIIRDNGD RIDLRFHPKP SDLHLQTGYK VERHMCDGDI VIFNRQPTLH KMSMMGHRVR ILPWS TFRL NLSVTTPYNA DFDGDEMNLH LPQSLETRAE IQELAMVPRM IVTPQSNRPV MGIVQDTLTA VRKFTKRDVF LERGEV MNL LMFLSTWDGK VPQPAILKPR PLWTGKQIFS LIIPGHINCI RTHSTHPDDE DSGPYKHISP GDTKVVVENG ELIMGIL CK KSLGTSAGSL VHISYLEMGH DITRLFYSNI QTVINNWLLI EGHTIGIGDS IADSKTYQDI QNTIKKAKQD VIEVIEKA H NNELEPTPGN TLRQTFENQV NRILNDARDK TGSSAQKSLS EYNNFKSMVV SGAKGSKINI SQVIAVVGQQ NVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQL RYGEDGLAGE SVEFQNLATL KPSNKAFEKK FRFDYTNERA LRRTLQEDLV KDVLSNAHIQ NELEREFERM R EDREVLRV IFPTGDSKVV LPCNLLRMIW NAQKIFHINP RLPSDLHPIK VVEGVKELSK KLVIVNGDDP LSRQAQENAT LL FNIHLRS TLCSRRMAEE FRLSGEAFDW LLGEIESKFN QAIAHPGEMV GALAAQSLGE PATQMTLNTF HYAGVSAKNV TLG VPRLKE LINISKKPKT PSLTVFLLGQ SARDAERAKD ILCRLEHTTL RKVTANTAIY YDPNPQSTVV AEDQEWVNVY YEMP DFDVA RISPWLLRVE LDRKHMTDRK LTMEQIAEKI NAGFGDDLNC IFNDDNAEKL VLRIRIMNSD ENKMQEEEEV VDKMD DDVF LRCIESNMLT DMTLQGIEQI SKVYMHLPQT DNKKKIIITE DGEFKALQEW ILETDGVSLM RVLSEKDVDP VRTTSN DIV EIFTVLGIEA VRKALERELY HVISFDGSYV NYRHLALLCD TMTCRGHLMA ITRHGVNRQD TGPLMKCSFE ETVDVLM EA AAHGESDPMK GVSENIMLGQ LAPAGTGCFD LLLDAEKCKY GMEIPTNIPG LGAAGPTGMF FGSAPSPMGG ISPAMTPW N QGATPAYGAW SPSVGSGMTP GAAGFSPSAA SDASGFSPGY SPAWSPTPGS PGSPGPSSPY IPSPGGAMSP SYSPTSPAY EPRSPGGYTP QSPSYSPTSP SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPNYS PTSPNYTPTS P SYSPTSPS YSPTSPNYTP TSPNYSPTSP SYSPTSPSYS PTSPSYSPSS PRYTPQSPTY TPSSPSYSPS SPSYSPTSPK YT PTSPSYS PSSPEYTPTS PKYSPTSPKY SPTSPKYSPT SPTYSPTTPK YSPTSPTYSP TSPVYTPTSP KYSPTSPTYS PTS PKYSPT SPTYSPTSPK GSTYSPTSPG YSPTSPTYSL TSPAISPDDS DEEN

UniProtKB: DNA-directed RNA polymerase II subunit RPB1

Macromolecule #2: DNA-directed RNA polymerase subunit beta

• Macromolecule: Name: DNA-directed RNA polymerase subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 134.041422 KDa

Sequence

String:

MYDADEDMQY DEDDDEITPD LWQEACWIVI SSYFDEKGLV RQQLDSFDEF IQMSVQRIVE DAPPIDLQAE AQHASGEVEE PPRYLLKFE QIYLSKPTHW ERDGAPSPMM PNEARLRNLT YSAPLYVDIT KTVIKEGEEQ LQTQHQKTFI GKIPIMLRST Y CLLNGLTD RDLCELNECP LDPGGYFIIN GSEKVLIAQE KMATNTVYVF AKKDSKYAYT GECRSCLENS SRPTSTIWVS ML ARGGQGA KKSAIGQRIV ATLPYIKQEV PIIIVFRALG FVSDRDILEH IIYDFEDPEM MEMVKPSLDE AFVIQEQNVA LNF IGSRGA KPGVTKEKRI KYAKEVLQKE MLPHVGVSDF CETKKAYFLG YMVHRLLLAA LGRRELDDRD HYGNKRLDLA GPLL AFLFR GMFKNLLKEV RIYAQKFIDR GKDFNLELAI KTRIISDGLK YSLATGNWGD QKKAHQARAG VSQVLNRLTF ASTLS HLRR LNSPIGRDGK LAKPRQLHNT LWGMVCPAET PEGHAVGLVK NLALMAYISV GSQPSPILEF LEEWSMENLE EISPAA IAD ATKIFVNGCW VGIHKDPEQL MNTLRKLRRQ MDIIVSEVSM IRDIREREIR IYTDAGRICR PLLIVEKQKL LLKKRHI DQ LKEREYNNYS WQDLVASGVV EYIDTLEEET VMLAMTPDDL QEKEVAYCST YTHCEIHPSM ILGVCASIIP FPDHNQSP R NTYQSAMGKQ AMGVYITNFH VRMDTLAHVL YYPQKPLVTT RSMEYLRFRE LPAGINSIVA IASYTGYNQE DSVIMNRSA VDRGFFRSVF YRSYKEQESK KGFDQEEVFE KPTRETCQGM RHAIYDKLDD DGLIAPGVRV SGDDVIIGKT VTLPENEDEL EGTNRRYTK RDCSTFLRTS ETGIVDQVMV TLNQEGYKFC KIRVRSVRIP QIGDKFASRH GQKGTCGIQY RQEDMPFTCE G ITPDIIIN PHAIPSRMTI GHLIECLQGK VSANKGEIGD ATPFNDAVNV QKISNLLSDY GYHLRGNEVL YNGFTGRKIT SQ IFIGPTY YQRLKHMVDD KIHSRARGPI QILNRQPMEG RSRDGGLRFG EMERDCQIAH GAAQFLRERL FEASDPYQVH VCN LCGIMA IANTRTHTYE CRGCRNKTQI SLVRMPYACK LLFQELMSMS IAPRMMSV

UniProtKB: DNA-directed RNA polymerase subunit beta

Macromolecule #3: DNA-directed RNA polymerase II subunit RPB3

• Macromolecule: Name: DNA-directed RNA polymerase II subunit RPB3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 31.439074 KDa

Sequence

String:

MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH DEFIAHRLGL IPLTSDDIVD KLQYSRDCT CEEFCPECSV EFTLDVRCNE DQTRHVTSRD LISNSPRVIP VTSRNRDNDP SDYVEQDDIL IVKLRKGQEL R LRAYAKKG FGKEHAKWNP TAGVAFEYDP DNALRHTVYP KPEEWPKSEY SELDEDESQA PYDPNGKPER FYYNVESCGS LR PETIVLS ALSGLKKKLS DLQTQLSHEI QSDVLTIN

UniProtKB: DNA-directed RNA polymerase II subunit RPB3

Macromolecule #4: RPOL4c domain-containing protein

• Macromolecule: Name: RPOL4c domain-containing protein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 16.331255 KDa

Sequence

String:

MAAGGSDPRA GDVEEDASQL IFPKEFETAE TLLNSEVHML LEHRKQQNES AEDEQELSEV FMKTLNYTAR FSRFKNRETI ASVRSLLLQ KKLHKFELAC LANLCPETAE ESKALIPSLE GRFEDEELQQ ILDDIQTKRS FQY

UniProtKB: DNA-directed RNA polymerase II subunit RPB4

Macromolecule #5: DNA-directed RNA polymerase II subunit E

• Macromolecule: Name: DNA-directed RNA polymerase II subunit E / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 24.644318 KDa

Sequence

String:

MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQFGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN QLPRIQAGDP VARYFGIKRG QVVKIIRPSE TAGRYITYRL VQ

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC1

Macromolecule #6: DNA-directed RNA polymerase II subunit F

• Macromolecule: Name: DNA-directed RNA polymerase II subunit F / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 14.477001 KDa

Sequence

String:

MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY ERARVLGTRA LQIAMCAPVM VELEGETDP LLIAMKELKA RKIPIIIRRY LPDGSYEDWG VDELIISD

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC2

Macromolecule #7: DNA-directed RNA polymerase II subunit RPB7

• Macromolecule: Name: DNA-directed RNA polymerase II subunit RPB7 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 19.314283 KDa

Sequence

String:

MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ PGRGFVLYPV KYKAIVFRPF KGEVVDAVV TQVNKVGLFT EIGPMSCFIS RHSIPSEMEF DPNSNPPCYK TMDEDIVIQQ DDEIRLKIVG TRVDKNDIFA I GSLMDDYL GLVS

UniProtKB: DNA-directed RNA polymerase II subunit RPB7

Macromolecule #8: DNA-directed RNA polymerases I, II, and III subunit RPABC3

• Macromolecule: Name: DNA-directed RNA polymerases I, II, and III subunit RPABC3; type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 17.162273 KDa

Sequence

String:

MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI ASTLYEDGTL DDGEYNPTDD RPSRADQFE YVMYGKVYRI EGDETSTEAA TRLSAYVSYG GLLMRLQGDA NNLHGFEVDS RVYLLMKKLA F

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC3

Macromolecule #9: DNA-directed RNA polymerase II subunit RPB9

• Macromolecule: Name: DNA-directed RNA polymerase II subunit RPB9 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 14.541221 KDa

Sequence

String:

MEPDGTYEPG FVGIRFCQEC NNMLYPKEDK ENRILLYACR NCDYQQEADN SCIYVNKITH EVDELTQIIA DVSQDPTLPR TEDHPCQKC GHKEAVFFQS HSARAEDAMR LYYVCTAPHC GHRWTE

UniProtKB: DNA-directed RNA polymerase II subunit RPB9

Macromolecule #10: DNA-directed RNA polymerases I, II, and III subunit RPABC5

• Macromolecule: Name: DNA-directed RNA polymerases I, II, and III subunit RPABC5; type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 7.655123 KDa

Sequence

String:

MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL NYAPLEK

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC5

Macromolecule #11: RNA_pol_L_2 domain-containing protein

• Macromolecule: Name: RNA_pol_L_2 domain-containing protein / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 13.310284 KDa

Sequence

String:

MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG YKVPHPLEHK IIIRVQTTPD YSPQEAFTN AITDLISELS LLEERFRVAI KDKQEGIE

UniProtKB: DNA-directed RNA polymerase RBP11-like dimerisation domain-containing protein

Macromolecule #12: RNA polymerase II subunit K

• Macromolecule: Name: RNA polymerase II subunit K / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Sus scrofa (pig)
• Molecular weight: Theoretical: 7.018244 KDa

Sequence

String:

MDTQKDVQPP KQQPMIYICG ECHTENEIKS RDPIRCRECG YRIMYKKRTK RLVVFDAR

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC4

Macromolecule #16: DNA excision repair protein ERCC-8

• Macromolecule: Name: DNA excision repair protein ERCC-8 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 44.10716 KDa
• Recombinant expression: Organism: Trichoplusia ni (cabbage looper)

Sequence

String:

MLGFLSARQT GLEDPLRLRR AESTRRVLGL ELNKDRDVER IHGGGINTLD IEPVEGRYML SGGSDGVIVL YDLENSSRQS YYTCKAVCS IGRDHPDVHR YSVETVQWYP HDTGMFTSSS FDKTLKVWDT NTLQTADVFN FEETVYSHHM SPVSTKHCLV A VGTRGPKV QLCDLKSGSC SHILQGHRQE ILAVSWSPRY DYILATASAD SRVKLWDVRR ASGCLITLDQ HNGKKSQAVE SA NTAHNGK VNGLCFTSDG LHLLTVGTDN RMRLWNSSNG ENTLVNYGKV CNNSKKGLKF TVSCGCSSEF VFVPYGSTIA VYT VYSGEQ ITMLKGHYKT VDCCVFQSNF QELYSGSRDC NILAWVPSLY EPVPDDDETT TKSQLNPAFE DAWSSSDEEG

UniProtKB: DNA excision repair protein ERCC-8

Macromolecule #17: DNA excision repair protein ERCC-6

• Macromolecule: Name: DNA excision repair protein ERCC-6 / type: protein_or_peptide / ID: 17 / 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: Homo sapiens (human)
• Molecular weight: Theoretical: 168.673547 KDa
• Recombinant expression: Organism: Trichoplusia ni (cabbage looper)

Sequence

String:

MPNEGIPHSS QTQEQDCLQS QPVSNNEEMA IKQESGGDGE VEEYLSFRSV GDGLSTSAVG CASAAPRRGP ALLHIDRHQI QAVEPSAQA LELQGLGVDV YDQDVLEQGV LQQVDNAIHE ASRASQLVDV EKEYRSVLDD LTSCTTSLRQ INKIIEQLSP Q AATSRDIN RKLDSVKRQK YNKEQQLKKI TAKQKHLQAI LGGAEVKIEL DHASLEEDAE PGPSSLGSML MPVQETAWEE LI RTGQMTP FGTQIPQKQE KKPRKIMLNE ASGFEKYLAD QAKLSFERKK QGCNKRAARK APAPVTPPAP VQNKNKPNKK ARV LSKKEE RLKKHIKKLQ KRALQFQGKV GLPKARRPWE SDMRPEAEGD SEGEESEYFP TEEEEEEEDD EVEGAEADLS GDGT DYELK PLPKGGKRQK KVPVQEIDDD FFPSSGEEAE AASVGEGGGG GRKVGRYRDD GDEDYYKQRL RRWNKLRLQD KEKRL KLED DSEESDAEFD EGFKVPGFLF KKLFKYQQTG VRWLWELHCQ QAGGILGDEM GLGKTIQIIA FLAGLSYSKI RTRGSN YRF EGLGPTVIVC PTTVMHQWVK EFHTWWPPFR VAILHETGSY THKKEKLIRD VAHCHGILIT SYSYIRLMQD DISRYDW HY VILDEGHKIR NPNAAVTLAC KQFRTPHRII LSGSPMQNNL RELWSLFDFI FPGKLGTLPV FMEQFSVPIT MGGYSNAS P VQVKTAYKCA CVLRDTINPY LLRRMKSDVK MSLSLPDKNE QVLFCRLTDE QHKVYQNFVD SKEVYRILNG EMQIFSGLI ALRKICNHPD LFSGGPKNLK GLPDDELEED QFGYWKRSGK MIVVESLLKI WHKQGQRVLL FSQSRQMLDI LEVFLRAQKY TYLKMDGTT TIASRQPLIT RYNEDTSIFV FLLTTRVGGL GVNLTGANRV VIYDPDWNPS TDTQARERAW RIGQKKQVTV Y RLLTAGTI EEKIYHRQIF KQFLTNRVLK DPKQRRFFKS NDLYELFTLT SPDASQSTET SAIFAGTGSD VQTPKCHLKR RI QPAFGAD HDVPKRKKFP ASNISVNDAT SSEEKSEAKG AEVNAVTSNR SDPLKDDPHM SSNVTSNDRL GEETNAVSGP EEL SVISGN GECSNSSGTG KTSMPSGDES IDEKLGLSYK RERPSQAQTE AFWENKQMEN NFYKHKSKTK HHSVAEEETL EKHL RPKQK PKNSKHCRDA KFEGTRIPHL VKKRRYQKQD SENKSEAKEQ SNDDYVLEKL FKKSVGVHSV MKHDAIMDGA SPDYV LVEA EANRVAQDAL KALRLSRQRC LGAVSGVPTW TGHRGISGAP AGKKSRFGKK RNSNFSVQHP SSTSPTEKCQ DGIMKK EGK DNVPEHFSGR AEDADSSSGP LASSSLLAKM RARNHLILPE RLESESGHLQ EASALLPTTE HDDLLVEMRN FIAFQAH TD GQASTREILQ EFESKLSASQ SCVFRELLRN LCTFHRTSGG EGIWKLKPEY C

UniProtKB: DNA excision repair protein ERCC-6

Macromolecule #18: CSB element

• Macromolecule: Name: CSB element / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 2.996685 KDa
• Recombinant expression: Organism: Trichoplusia ni (cabbage looper)

Sequence

String:

(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)

Macromolecule #19: UV-stimulated scaffold protein A

• Macromolecule: Name: UV-stimulated scaffold protein A / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 80.72168 KDa
• Recombinant expression: Organism: Trichoplusia ni (cabbage looper)

Sequence

String:

MDQKLSKLVE ELTTSGEPRL NPEKMKELKK ICKSSEEQLS RAYRLLIAQL TQEHAEIRLS AFQIVEELFV RSHQFRMLVV SNFQEFLEL TLGTDPAQPL PPPREAAQRL RQATTRAVEG WNEKFGEAYK KLALGYHFLR HNKKVDFQDT NARSLAERKR E EEKQKHLD KIYQERASQA EREMQEMSGE IESCLTEVES CFRLLVPFDF DPNPETESLG MASGMSDALR SSCAGQVGPC RS GTPDPRD GEQPCCSRDL PASAGHPRAG GGAQPSQTAT GDPSDEDEDS DLEEFVRSHG LGSHKYTLDV ELCSEGLKVQ ENE DNLALI HAARDTLKLI RNKFLPAVCS WIQRFTRVGT HGGCLKRAID LKAELELVLR KYKELDIEPE GGERRRTEAL GDAE EDEDD EDFVEVPEKE GYEPHIPDHL RPEYGLEAAP EKDTVVRCLR TRTRMDEEVS DPTSAAAQLR QLRDHLPPPS SASPS RALP EPQEAQKLAA ERARAPVVPY GVDLHYWGQE LPTAGKIVKS DSQHRFWKPS EVEEEVVNAD ISEMLRSRHI TFAGKF EPV QHWCRAPRPD GRLCERQDRL KCPFHGKIVP RDDEGRPLDP EDRAREQRRQ LQKQERPEWQ DPELMRDVEA ATGQDLG SS RYSGKGRGKK RRYPSLTNLK AQADTARARI GRKVFAKAAV RRVVAAMNRM DQKKHEKFSN QFNYALN

UniProtKB: UV-stimulated scaffold protein A

Macromolecule #20: DNA damage-binding protein 1

• Macromolecule: Name: DNA damage-binding protein 1 / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 127.369719 KDa
• Recombinant expression: Organism: Trichoplusia ni (cabbage looper)

Sequence

String:

SNAMSYNYVV TAQKPTAVNG CVTGHFTSAE DLNLLIAKNT RLEIYVVTAE GLRPVKEVGM YGKIAVMELF RPKGESKDLL FILTAKYNA CILEYKQSGE SIDIITRAHG NVQDRIGRPS ETGIIGIIDP ECRMIGLRLY DGLFKVIPLD RDNKELKAFN I RLEELHVI DVKFLYGCQA PTICFVYQDP QGRHVKTYEV SLREKEFNKG PWKQENVEAE ASMVIAVPEP FGGAIIIGQE SI TYHNGDK YLAIAPPIIK QSTIVCHNRV DPNGSRYLLG DMEGRLFMLL LEKEEQMDGT VTLKDLRVEL LGETSIAECL TYL DNGVVF VGSRLGDSQL VKLNVDSNEQ GSYVVAMETF TNLGPIVDMC VVDLERQGQG QLVTCSGAFK EGSLRIIRNG IGIH EHASI DLPGIKGLWP LRSDPNRETD DTLVLSFVGQ TRVLMLNGEE VEETELMGFV DDQQTFFCGN VAHQQLIQIT SASVR LVSQ EPKALVSEWK EPQAKNISVA SCNSSQVVVA VGRALYYLQI HPQELRQISH TEMEHEVACL DITPLGDSNG LSPLCA IGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTV LR TFRSLSTTNV FACSDRPTVI YSSNHKLVFS NVNLKEVNYM CPLNSDGYPD SLALANNSTL TIGTIDEIQK LHIRTVPL Y ESPRKICYQE VSQCFGVLSS RIEVQDTSGG TTALRPSAST QALSSSVSSS KLFSSSTAPH ETSFGEEVEV HNLLIIDQH TFEVLHAHQF LQNEYALSLV SCKLGKDPNT YFIVGTAMVY PEEAEPKQGR IVVFQYSDGK LQTVAEKEVK GAVYSMVEFN GKLLASINS TVRLYEWTTE KELRTECNHY NNIMALYLKT KGDFILVGDL MRSVLLLAYK PMEGNFEEIA RDFNPNWMSA V EILDDDNF LGAENAFNLF VCQKDSAATT DEERQHLQEV GLFHLGEFVN VFCHGSLVMQ NLGETSTPTQ GSVLFGTVNG MI GLVTSLS ESWYNLLLDM QNRLNKVIKS VGKIEHSFWR SFHTERKTEP ATGFIDGDLI ESFLDISRPK MQEVVANLQY DDG SGMKRE ATADDLIKVV EELTRIH

UniProtKB: DNA damage-binding protein 1

Macromolecule #13: NTS

• Macromolecule: Name: NTS / type: dna / ID: 13 / Number of copies: 1 / Classification: DNA
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 14.494314 KDa

Sequence

String:

(DC)(DT)(DA)(DG)(DT)(DT)(DG)(DA)(DT)(DC) (DT)(DC)(DA)(DT)(DA)(DT)(DT)(DT)(DC)(DA) (DT)(DT)(DC)(DC)(DT)(DA)(DC)(DT)(DC) (DA)(DG)(DG)(DA)(DG)(DA)(DA)(DG)(DG)(DA) (DG) (DC)(DA)(DG)(DA)(DG)(DC)(DG)

Macromolecule #14: TS

• Macromolecule: Name: TS / type: dna / ID: 14 / Number of copies: 1 / Classification: DNA
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 14.269129 KDa

Sequence

String:

(DC)(DG)(DC)(DT)(DC)(DT)(DG)(DC)(DT)(DC) (DC)(DT)(DT)(DC)(DT)(DC)(DC)(DC)(DA)(DT) (DC)(DC)(DT)(DC)(DT)(DC)(DG)(DA)(DT) (DG)(DG)(DC)(DT)(DA)(DT)(DG)(DA)(DG)(DA) (DT) (DC)(DA)(DA)(DC)(DT)(DA)(DG)

Macromolecule #15: RNA

• Macromolecule: Name: RNA / type: rna / ID: 15 / Number of copies: 1
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 3.264036 KDa

Sequence

String:

AUCGAGAGGA

Macromolecule #21: ZINC ION

• Macromolecule: Name: ZINC ION / type: ligand / ID: 21 / Number of copies: 8 / Formula: ZN
• Molecular weight: Theoretical: 65.409 Da

Macromolecule #22: MAGNESIUM ION

• Macromolecule: Name: MAGNESIUM ION / type: ligand / ID: 22 / Number of copies: 1 / Formula: MG
• Molecular weight: Theoretical: 24.305 Da

Experimental details

Structure determination

• Method: cryo EM
• Processing: single particle reconstruction
• Aggregation state: particle

Sample preparation

• Concentration: 0.3 mg/mL
• Buffer: pH: 7.5
• Grid: Model: Quantifoil R2/1 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
• Vitrification: Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

Electron microscopy

• Microscope: FEI TITAN KRIOS
• Image recording: Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 10300 / Average electron dose: 40.4 e/Ų
• Electron beam: Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
• Electron optics: Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
• Experimental equipment: Model: Titan Krios / Image courtesy: FEI Company

Image processing

• Particle selection: Number selected: 2527839
• CTF correction: Software - Name: Warp / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
• Startup model: Type of model: EMDB MAP
• Final reconstruction: Resolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF; Details: Number of particles is different for every focused refined map, as detailed in the manuscript.; Number images used: 100000
• Initial angle assignment: Type: PROJECTION MATCHING / Software - Name: cryoSPARC
• Final angle assignment: Type: PROJECTION MATCHING / Software - Name: RELION