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- EMDB-41502: Structure of the human CDK8 kinase module -

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Basic information

Entry
Database: EMDB / ID: EMD-41502
TitleStructure of the human CDK8 kinase module
Map data
Sample
  • Complex: human CDK8 kinase module
    • Protein or peptide: Mediator of RNA polymerase II transcription subunit 12
    • Protein or peptide: Mediator of RNA polymerase II transcription subunit 13
    • Protein or peptide: Cyclin-dependent kinase 8
    • Protein or peptide: Cyclin-C
  • Ligand: ZINC ION
KeywordsTranscription / Mediator / CDK8 / MED12 / MED13 / CKM.
Function / homology
Function and homology information


axis elongation involved in somitogenesis / CKM complex / embryonic neurocranium morphogenesis / G0 to G1 transition / oligodendrocyte development / post-anal tail morphogenesis / endoderm development / embryonic brain development / mediator complex / RNA polymerase II CTD heptapeptide repeat Y1 kinase activity ...axis elongation involved in somitogenesis / CKM complex / embryonic neurocranium morphogenesis / G0 to G1 transition / oligodendrocyte development / post-anal tail morphogenesis / endoderm development / embryonic brain development / mediator complex / RNA polymerase II CTD heptapeptide repeat Y1 kinase activity / RNA polymerase II CTD heptapeptide repeat S2 kinase activity / RNA polymerase II CTD heptapeptide repeat T4 kinase activity / RNA polymerase II CTD heptapeptide repeat S5 kinase activity / RNA polymerase II CTD heptapeptide repeat S7 kinase activity / Generic Transcription Pathway / triglyceride homeostasis / nuclear vitamin D receptor binding / [RNA-polymerase]-subunit kinase / nuclear thyroid hormone receptor binding / Wnt signaling pathway, planar cell polarity pathway / cyclin-dependent protein serine/threonine kinase regulator activity / spinal cord development / RSV-host interactions / somatic stem cell population maintenance / negative regulation of Notch signaling pathway / positive regulation of transcription initiation by RNA polymerase II / ubiquitin ligase complex / cyclin-dependent kinase / cyclin-dependent protein serine/threonine kinase activity / Schwann cell development / cyclin-dependent protein kinase holoenzyme complex / cholesterol homeostasis / transcription coregulator activity / neural tube closure / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / PPARA activates gene expression / beta-catenin binding / Transcriptional regulation of white adipocyte differentiation / NOTCH1 Intracellular Domain Regulates Transcription / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / ubiquitin protein ligase activity / heart development / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / transcription coactivator activity / protein kinase activity / protein ubiquitination / RNA polymerase II cis-regulatory region sequence-specific DNA binding / protein serine kinase activity / protein serine/threonine kinase activity / chromatin binding / positive regulation of DNA-templated transcription / nucleolus / positive regulation of transcription by RNA polymerase II / protein-containing complex / nucleoplasm / ATP binding / identical protein binding / nucleus / membrane
Similarity search - Function
Mediator complex, subunit Med12, catenin-binding / Mediator complex, subunit Med12, LCEWAV-domain / : / Eukaryotic Mediator 12 catenin-binding domain / Eukaryotic Mediator 12 subunit domain / Mediator complex, subunit Med12 / MID domain of medPIWI / Transcription mediator complex subunit Med12 / MID domain of medPIWI / Transcription mediator complex subunit Med12 ...Mediator complex, subunit Med12, catenin-binding / Mediator complex, subunit Med12, LCEWAV-domain / : / Eukaryotic Mediator 12 catenin-binding domain / Eukaryotic Mediator 12 subunit domain / Mediator complex, subunit Med12 / MID domain of medPIWI / Transcription mediator complex subunit Med12 / MID domain of medPIWI / Transcription mediator complex subunit Med12 / Mediator complex subunit Med13, C-terminal / : / Mediator complex subunit 13 C-terminal domain / Cyclin, C-terminal domain 2 / Cyclin C-terminal domain / Cyclin/Cyclin-like subunit Ssn8 / Cyclin, N-terminal / Cyclin, N-terminal domain / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Cyclin-like superfamily / : / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Cyclin-C / Cyclin-dependent kinase 8 / Mediator of RNA polymerase II transcription subunit 12 / Mediator of RNA polymerase II transcription subunit 13
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsChen SF / Chao TC / Kim HJ / Tang HC / Khadka S / Li T / Murakami K / Boyer TG / Tsai KL
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: Mol Cell / Year: 2024
Title: Structural basis of the human transcriptional Mediator regulated by its dissociable kinase module.
Authors: Ti-Chun Chao / Shin-Fu Chen / Hee Jong Kim / Hui-Chi Tang / Hsiang-Ching Tseng / An Xu / Leon Palao / Subash Khadka / Tao Li / Mo-Fan Huang / Dung-Fang Lee / Kenji Murakami / Thomas G Boyer / Kuang-Lei Tsai /
Abstract: The eukaryotic transcriptional Mediator comprises a large core (cMED) and a dissociable CDK8 kinase module (CKM). cMED recruits RNA polymerase II (RNA Pol II) and promotes pre-initiation complex ...The eukaryotic transcriptional Mediator comprises a large core (cMED) and a dissociable CDK8 kinase module (CKM). cMED recruits RNA polymerase II (RNA Pol II) and promotes pre-initiation complex formation in a manner repressed by the CKM through mechanisms presently unknown. Herein, we report cryoelectron microscopy structures of the complete human Mediator and its CKM. The CKM binds to multiple regions on cMED through both MED12 and MED13, including a large intrinsically disordered region (IDR) in the latter. MED12 and MED13 together anchor the CKM to the cMED hook, positioning CDK8 downstream and proximal to the transcription start site. Notably, the MED13 IDR obstructs the recruitment of RNA Pol II/MED26 onto cMED by direct occlusion of their respective binding sites, leading to functional repression of cMED-dependent transcription. Combined with biochemical and functional analyses, these structures provide a conserved mechanistic framework to explain the basis for CKM-mediated repression of cMED function.
History
DepositionAug 6, 2023-
Header (metadata) releaseOct 9, 2024-
Map releaseOct 9, 2024-
UpdateMay 21, 2025-
Current statusMay 21, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_41502.png

Downloads & links

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Map

FileDownload / File: emd_41502.map.gz / Format: CCP4 / Size: 166.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 352 pix.
= 376.675 Å		1.07 Å/pix.
x 352 pix.
= 376.675 Å		1.07 Å/pix.
x 352 pix.
= 376.675 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.0701 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0115
Minimum - Maximum-0.047040742 - 0.09838468
Average (Standard dev.)0.00007991853 (±0.0024259202)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions352352352
Spacing352352352
CellA=B=C: 376.67517 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_41502_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_41502_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : human CDK8 kinase module

EntireName: human CDK8 kinase module
Components
  • Complex: human CDK8 kinase module
    • Protein or peptide: Mediator of RNA polymerase II transcription subunit 12
    • Protein or peptide: Mediator of RNA polymerase II transcription subunit 13
    • Protein or peptide: Cyclin-dependent kinase 8
    • Protein or peptide: Cyclin-C
  • Ligand: ZINC ION

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Supramolecule #1: human CDK8 kinase module

SupramoleculeName: human CDK8 kinase module / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Mediator of RNA polymerase II transcription subunit 12

MacromoleculeName: Mediator of RNA polymerase II transcription subunit 12
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 243.354891 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MAAFGILSYE HRPLKRPRLG PPDVYPQDPK QKEDELTALN VKQGFNNQPA VSGDEHGSAK NVSFNPAKIS SNFSSIIAEK LRCNTLPDT GRRKPQVNQK DNFWLVTARS QSAINTWFTD LAGTKPLTQL AKKVPIFSKK EEVFGYLAKY TVPVMRAAWL I KMTCAYYA ...String:
MAAFGILSYE HRPLKRPRLG PPDVYPQDPK QKEDELTALN VKQGFNNQPA VSGDEHGSAK NVSFNPAKIS SNFSSIIAEK LRCNTLPDT GRRKPQVNQK DNFWLVTARS QSAINTWFTD LAGTKPLTQL AKKVPIFSKK EEVFGYLAKY TVPVMRAAWL I KMTCAYYA AISETKVKKR HVDPFMEWTQ IITKYLWEQL QKMAEYYRPG PAGSGGCGST IGPLPHDVEV AIRQWDYTEK LA MFMFQDG MLDRHEFLTW VLECFEKIRP GEDELLKLLL PLLLRYSGEF VQSAYLSRRL AYFCTRRLAL QLDGVSSHSS HVI SAQSTS TLPTTPAPQP PTSSTPSTPF SDLLMCPQHR PLVFGLSCIL QTILLCCPSA LVWHYSLTDS RIKTGSPLDH LPIA PSNLP MPEGNSAFTQ QVRAKLREIE QQIKERGQAV EVRWSFDKCQ EATAGFTIGR VLHTLEVLDS HSFERSDFSN SLDSL CNRI FGLGPSKDGH EISSDDDAVV SLLCEWAVSC KRSGRHRAMV VAKLLEKRQA EIEAERCGES EAADEKGSIA SGSLSA PSA PIFQDVLLQF LDTQAPMLTD PRSESERVEF FNLVLLFCEL IRHDVFSHNM YTCTLISRGD LAFGAPGPRP PSPFDDP AD DPEHKEAEGS SSSKLEDPGL SESMDIDPSS SVLFEDMEKP DFSLFSPTMP CEGKGSPSPE KPDVEKEVKP PPKEKIEG T LGVLYDQPRH VQYATHFPIP QEESCSHECN QRLVVLFGVG KQRDDARHAI KKITKDILKV LNRKGTAETD QLAPIVPLN PGDLTFLGGE DGQKRRRNRP EAFPTAEDIF AKFQHLSHYD QHQVTAQVSR NVLEQITSFA LGMSYHLPLV QHVQFIFDLM EYSLSISGL IDFAIQLLNE LSVVEAELLL KSSDLVGSYT TSLCLCIVAV LRHYHACLIL NQDQMAQVFE GLCGVVKHGM N RSDGSSAE RCILAYLYDL YTSCSHLKNK FGELFSDFCS KVKNTIYCNV EPSESNMRWA PEFMIDTLEN PAAHTFTYTG LG KSLSENP ANRYSFVCNA LMHVCVGHHD PDRVNDIAIL CAELTGYCKS LSAEWLGVLK ALCCSSNNGT CGFNDLLCNV DVS DLSFHD SLATFVAILI ARQCLLLEDL IRCAAIPSLL NAACSEQDSE PGARLTCRIL LHLFKTPQLN PCQSDGNKPT VGIR SSCDR HLLAASQNRI VDGAVFAVLK AVFVLGDAEL KGSGFTVTGG TEELPEEEGG GGSGGRRQGG RNISVETASL DVYAK YVLR SICQQEWVGE RCLKSLCEDS NDLQDPVLSS AQAQRLMQLI CYPHRLLDNE DGENPQRQRI KRILQNLDQW TMRQSS LEL QLMIKQTPNN EMNSLLENIA KATIEVFQQS AETGSSSGST ASNMPSSSKT KPVLSSLERS GVWLVAPLIA KLPTSVQ GH VLKAAGEELE KGQHLGSSSR KERDRQKQKS MSLLSQQPFL SLVLTCLKGQ DEQREGLLTS LYSQVHQIVN NWRDDQYL D DCKPKQLMHE ALKLRLNLVG GMFDTVQRST QQTTEWAMLL LEIIISGTVD MQSNNELFTT VLDMLSVLIN GTLAADMSS ISQGSMEENK RAYMNLAKKL QKELGERQSD SLEKVRQLLP LPKQTRDVIT CEPQGSLIDT KGNKIAGFDS IFKKEGLQVS TKQKISPWD LFEGLKPSAP LSWGWFGTVR VDRRVARGEE QQRLLLYHTH LRPRPRAYYL EPLPLPPEDE EPPAPTLLEP E KKAPEPPK TDKPGAAPPS TEERKKKSTK GKKRSQPATK TEDYGMGPGR SGPYGVTVPP DLLHHPNPGS ITHLNYRQGS IG LYTQNQP LPAGGPRVDP YRPVRLPMQK LPTRPTYPGV LPTTMTGVMG LEPSSYKTSV YRQQQPAVPQ GQRLRQQLQQ SQG MLGQSS VHQMTPSSSY GLQTSQGYTP YVSHVGLQQH TGPAGTMVPP SYSSQPYQST HPSTNPTLVD PTRHLQQRPS GYVH QQAPT YGHGLTSTQR FSHQTLQQTP MISTMTPMSA QGVQAGVRST AILPEQQQQQ QQQQQQQQQQ QQQQQQQQQQ QYHIR QQQQ QQILRQQQQQ QQQQQQQQQQ QQQQQQQQQQ QHQQQQQQQA APPQPQPQSQ PQFQRQGLQQ TQQQQQTAAL VRQLQQ QLS NTQPQPSTNI FGRY

UniProtKB: Mediator of RNA polymerase II transcription subunit 12

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Macromolecule #2: Mediator of RNA polymerase II transcription subunit 13

MacromoleculeName: Mediator of RNA polymerase II transcription subunit 13
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 239.535906 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MSASFVPNGA SLEDCHCNLF CLADLTGIKW KKYVWQGPTS APILFPVTEE DPILSSFSRC LKADVLGVWR RDQRPGRREL WIFWWGEDP SFADLIHHDL SEEEDGVWEN GLSYECRTLL FKAVHNLLER CLMNRNFVRI GKWFVKPYEK DEKPINKSEH L SCSFTFFL ...String:
MSASFVPNGA SLEDCHCNLF CLADLTGIKW KKYVWQGPTS APILFPVTEE DPILSSFSRC LKADVLGVWR RDQRPGRREL WIFWWGEDP SFADLIHHDL SEEEDGVWEN GLSYECRTLL FKAVHNLLER CLMNRNFVRI GKWFVKPYEK DEKPINKSEH L SCSFTFFL HGDSNVCTSV EINQHQPVYL LSEEHITLAQ QSNSPFQVIL CPFGLNGTLT GQAFKMSDSA TKKLIGEWKQ FY PISCCLK EMSEEKQEDM DWEDDSLAAV EVLVAGVRMI YPACFVLVPQ SDIPTPSPVG STHCSSSCLG VHQVPASTRD PAM SSVTLT PPTSPEEVQT VDPQSVQKWV KFSSVSDGFN SDSTSHHGGK IPRKLANHVV DRVWQECNMN RAQNKRKYSA SSGG LCEEA TAAKVASWDF VEATQRTNCS CLRHKNLKSR NAGQQGQAPS LGQQQQILPK HKTNEKQEKS EKPQKRPLTP FHHRV SVSD DVGMDADSAS QRLVISAPDS QVRFSNIRTN DVAKTPQMHG TEMANSPQPP PLSPHPCDVV DEGVTKTPST PQSQHF YQM PTPDPLVPSK PMEDRIDSLS QSFPPQYQEA VEPTVYVGTA VNLEEDEANI AWKYYKFPKK KDVEFLPPQL PSDKFKD DP VGPFGQESVT SVTELMVQCK KPLKVSDELV QQYQIKNQCL SAIASDAEQE PKIDPYAFVE GDEEFLFPDK KDRQNSER E AGKKHKVEDG TSSVTVLSHE EDAMSLFSPS IKQDAPRPTS HARPPSTSLI YDSDLAVSYT DLDNLFNSDE DELTPGSKK SANGSDDKAS CKESKTGNLD PLSCISTADL HKMYPTPPSL EQHIMGFSPM NMNNKEYGSM DTTPGGTVLE GNSSSIGAQF KIEVDEGFC SPKPSEIKDF SYVYKPENCQ ILVGCSMFAP LKTLPSQYLP PIKLPEECIY RQSWTVGKLE LLSSGPSMPF I KEGDGSNM DQEYGTAYTP QTHTSFGMPP SSAPPSNSGA GILPSPSTPR FPTPRTPRTP RTPRGAGGPA SAQGSVKYEN SD LYSPAST PSTCRPLNSV EPATVPSIPE AHSLYVNLIL SESVMNLFKD CNFDSCCICV CNMNIKGADV GVYIPDPTQE AQY RCTCGF SAVMNRKFGN NSGLFLEDEL DIIGRNTDCG KEAEKRFEAL RATSAEHVNG GLKESEKLSD DLILLLQDQC TNLF SPFGA ADQDPFPKSG VISNWVRVEE RDCCNDCYLA LEHGRQFMDN MSGGKVDEAL VKSSCLHPWS KRNDVSMQCS QDILR MLLS LQPVLQDAIQ KKRTVRPWGV QGPLTWQQFH KMAGRGSYGT DESPEPLPIP TFLLGYDYDY LVLSPFALPY WERLML EPY GSQRDIAYVV LCPENEALLN GAKSFFRDLT AIYESCRLGQ HRPVSRLLTD GIMRVGSTAS KKLSEKLVAE WFSQAAD GN NEAFSKLKLY AQVCRYDLGP YLASLPLDSS LLSQPNLVAP TSQSLITPPQ MTNTGNANTP SATLASAASS TMTVTSGV A ISTSVATANS TLTTASTSSS SSSNLNSGVS SNKLPSFPPF GSMNSNAAGS MSTQANTVQS GQLGGQQTSA LQTAGISGE SSSLPTQPHP DVSESTMDRD KVGIPTDGDS HAVTYPPAIV VYIIDPFTYE NTDESTNSSS VWTLGLLRCF LEMVQTLPPH IKSTVSVQI IPCQYLLQPV KHEDREIYPQ HLKSLAFSAF TQCRRPLPTS TNVKTLTGFG PGLAMETALR SPDRPECIRL Y APPFILAP VKDKQTELGE TFGEAGQKYN VLFVGYCLSH DQRWILASCT DLYGELLETC IINIDVPNRA RRKKSSARKF GL QKLWEWC LGLVQMSSLP WRVVIGRLGR IGHGELKDWS CLLSRRNLQS LSKRLKDMCR MCGISAADSP SILSACLVAM EPQ GSFVIM PDSVSTGSVF GRSTTLNMQT SQLNTPQDTS CTHILVFPTS ASVQVASATY TTENLDLAFN PNNDGADGMG IFDL LDTGD DLDPDIINIL PASPTGSPVH SPGSHYPHGG DAGKGQSTDR LLSTEPHEEV PNILQQPLAL GYFVSTAKAG PLPDW FWSA CPQAQYQCPL FLKASLHLHV PSVQSDELLH SKHSHPLDSN QTSDVLRFVL EQYNALSWLT CDPATQDRRS CLPIHF VVL NQLYNFIMNM L

UniProtKB: Mediator of RNA polymerase II transcription subunit 13

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Macromolecule #3: Cyclin-dependent kinase 8

MacromoleculeName: Cyclin-dependent kinase 8 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 53.368668 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MDYDFKVKLS SERERVEDLF EYEGCKVGRG TYGHVYKAKR KDGKDDKDYA LKQIEGTGIS MSACREIALL RELKHPNVIS LQKVFLSHA DRKVWLLFDY AEHDLWHIIK FHRASKANKK PVQLPRGMVK SLLYQILDGI HYLHANWVLH RDLKPANILV M GEGPERGR ...String:
MDYDFKVKLS SERERVEDLF EYEGCKVGRG TYGHVYKAKR KDGKDDKDYA LKQIEGTGIS MSACREIALL RELKHPNVIS LQKVFLSHA DRKVWLLFDY AEHDLWHIIK FHRASKANKK PVQLPRGMVK SLLYQILDGI HYLHANWVLH RDLKPANILV M GEGPERGR VKIADMGFAR LFNSPLKPLA DLDPVVVTFW YRAPELLLGA RHYTKAIDIW AIGCIFAELL TSEPIFHCRQ ED IKTSNPY HHDQLDRIFN VMGFPADKDW EDIKKMPEHS TLMKDFRRNT YTNCSLIKYM EKHKVKPDSK AFHLLQKLLT MDP IKRITS EQAMQDPYFL EDPLPTSDVF AGCQIPYPKR EFLTEEEPDD KGDKKNQQQQ QGNNHTNGTG HPGNQDSSHT QGPP LKKVR VVPPTTTSGG LIMTSDYQRS NPHAAYPNPG PSTSQPQSSM GYSATSQQPP QYSHQTHRY

UniProtKB: Cyclin-dependent kinase 8

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Macromolecule #4: Cyclin-C

MacromoleculeName: Cyclin-C / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 33.279691 KDa
Recombinant expressionOrganism: Baculovirus expression vector pFastBac1-HM
SequenceString: MAGNFWQSSH YLQWILDKQD LLKERQKDLK FLSEEEYWKL QIFFTNVIQA LGEHLKLRQQ VIATATVYFK RFYARYSLKS IDPVLMAPT CVFLASKVEE FGVVSNTRLI AAATSVLKTR FSYAFPKEFP YRMNHILECE FYLLELMDCC LIVYHPYRPL L QYVQDMGQ ...String:
MAGNFWQSSH YLQWILDKQD LLKERQKDLK FLSEEEYWKL QIFFTNVIQA LGEHLKLRQQ VIATATVYFK RFYARYSLKS IDPVLMAPT CVFLASKVEE FGVVSNTRLI AAATSVLKTR FSYAFPKEFP YRMNHILECE FYLLELMDCC LIVYHPYRPL L QYVQDMGQ EDMLLPLAWR IVNDTYRTDL CLLYPPFMIA LACLHVACVV QQKDARQWFA ELSVDMEKIL EIIRVILKLY EQ WKNFDER KEMATILSKM PKPKPPPNSE GEQGPNGSQN SSYSQS

UniProtKB: Cyclin-C

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Macromolecule #5: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 5 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 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

BufferpH: 7.9
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK III

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 64.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.6 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: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 122015
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: MAXIMUM LIKELIHOOD

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