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- EMDB-12559: Substrate receptor scaffolding module of yeast Chelator-GID SR4 E... -

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Basic information

Entry
Database: EMDB / ID: EMD-12559
TitleSubstrate receptor scaffolding module of yeast Chelator-GID SR4 E3 ubiquitin ligase bound to Fbp1 substrate
Map data
Sample
  • Complex: Substrate receptor scaffolding module of yeast Chelator-GID SR4 comprising Gid1, Gid4, Gid5, Gid8 and Gid9 bound to Fbp1
    • Protein or peptide: Vacuolar import and degradation protein 28
    • Protein or peptide: Glucose-induced degradation protein 8
    • Protein or peptide: BJ4_G0018240.mRNA.1.CDS.1
    • Protein or peptide: Protein FYV10
    • Protein or peptide: Vacuolar import and degradation protein 24
    • Protein or peptide: Fructose-bisphosphatase
KeywordsGID / CTLH / ubiquitin / E3 ligase / supramolecular assembly / metabolism / gluconeogenesis / cryoEM / LIGASE
Function / homology
Function and homology information


protein catabolic process in the vacuole / GID complex / Regulation of pyruvate metabolism / ascospore formation / traversing start control point of mitotic cell cycle / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / vacuole / negative regulation of gluconeogenesis / Neutrophil degranulation ...protein catabolic process in the vacuole / GID complex / Regulation of pyruvate metabolism / ascospore formation / traversing start control point of mitotic cell cycle / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / vacuole / negative regulation of gluconeogenesis / Neutrophil degranulation / ubiquitin protein ligase activity / proteasome-mediated ubiquitin-dependent protein catabolic process / carbohydrate metabolic process / nucleus / metal ion binding / cytoplasm
Similarity search - Function
Protein Fyv10/E3 ubiquitin-protein transferase MAEA / Armadillo-type fold containing protein ARMC8/Vid28 / Gid-type RING finger domain / Gid-type RING finger profile. / CRA domain / : / CT11-RanBPM / CTLH/CRA C-terminal to LisH motif domain / CTLH/CRA C-terminal to LisH motif domain / Vacuolar import/degradation protein Vid24 ...Protein Fyv10/E3 ubiquitin-protein transferase MAEA / Armadillo-type fold containing protein ARMC8/Vid28 / Gid-type RING finger domain / Gid-type RING finger profile. / CRA domain / : / CT11-RanBPM / CTLH/CRA C-terminal to LisH motif domain / CTLH/CRA C-terminal to LisH motif domain / Vacuolar import/degradation protein Vid24 / Vacuolar import and degradation protein / C-terminal to LisH motif. / CTLH, C-terminal LisH motif / C-terminal to LisH (CTLH) motif profile. / Fructose-1,6-bisphosphatase / Fructose-1,6-bisphosphatase, active site / Fructose-1-6-bisphosphatase active site. / Fructose-1,6-bisphosphatase class 1 / Fructose-1-6-bisphosphatase class I, N-terminal / Fructose-1-6-bisphosphatase class 1, C-terminal / Fructose-1-6-bisphosphatase, N-terminal domain / Fructose-1-6-bisphosphatase, C-terminal domain / LIS1 homology (LisH) motif profile. / LIS1 homology motif / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / Domain in SPla and the RYanodine Receptor. / SPRY domain / Armadillo-like helical / Concanavalin A-like lectin/glucanase domain superfamily / Armadillo-type fold
Similarity search - Domain/homology
Fructose-bisphosphatase / Protein FYV10 / Vacuolar import and degradation protein 24 / BJ4_G0038950.mRNA.1.CDS.1 / Glucose-induced degradation protein 8 / Vacuolar import and degradation protein 28
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsSherpa D / Chrustowicz J / Prabu JR / Schulman BA
Funding support Germany, 2 items
OrganizationGrant numberCountry
European Research Council (ERC)789016-NEDD8Activate Germany
German Research Foundation (DFG)SCHU 3196/1-1 Germany
Citation
Journal: Mol Cell / Year: 2021
Title: GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme.
Authors: Dawafuti Sherpa / Jakub Chrustowicz / Shuai Qiao / Christine R Langlois / Laura A Hehl / Karthik Varma Gottemukkala / Fynn M Hansen / Ozge Karayel / Susanne von Gronau / J Rajan Prabu / ...Authors: Dawafuti Sherpa / Jakub Chrustowicz / Shuai Qiao / Christine R Langlois / Laura A Hehl / Karthik Varma Gottemukkala / Fynn M Hansen / Ozge Karayel / Susanne von Gronau / J Rajan Prabu / Matthias Mann / Arno F Alpi / Brenda A Schulman /
Abstract: How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex (mutation of which causes deficiency in glucose-induced degradation of ...How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex (mutation of which causes deficiency in glucose-induced degradation of gluconeogenic enzymes), we discover supramolecular chelate assembly as an E3 ligase strategy for targeting an oligomeric substrate. Cryoelectron microscopy (cryo-EM) structures show that, to bind the tetrameric substrate fructose-1,6-bisphosphatase (Fbp1), two minimally functional GID E3s assemble into the 20-protein Chelator-GID, which resembles an organometallic supramolecular chelate. The Chelator-GID assembly avidly binds multiple Fbp1 degrons so that multiple Fbp1 protomers are simultaneously ubiquitylated at lysines near the allosteric and substrate binding sites. Importantly, key structural and biochemical features, including capacity for supramolecular assembly, are preserved in the human ortholog, the CTLH E3. Based on our integrative structural, biochemical, and cell biological data, we propose that higher-order E3 ligase assembly generally enables multipronged targeting, capable of simultaneously incapacitating multiple protomers and functionalities of oligomeric substrates.
#1: Journal: Biorxiv / Year: 2021
Title: GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme
Authors: Sherpa D / Chrustowicz J / Qiao S / Langlois CR / Hehl LA / Gottemukkala KV / Hansen FM / Karayel O / Prabu JR / Mann M / Alpi AF / Schulman BA
History
DepositionMar 5, 2021-
Header (metadata) releaseMay 5, 2021-
Map releaseMay 5, 2021-
UpdateOct 23, 2024-
Current statusOct 23, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.045
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.045
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  • Surface view with fitted model
  • Atomic models: PDB-7ns3
  • Surface level: 0.045
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7ns3
  • Imaged by Jmol
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Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_12559.png

Downloads & links

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Map

FileDownload / File: emd_12559.map.gz / Format: CCP4 / Size: 91.1 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.)
1.58 Å/pix.
x 288 pix.
= 455.04 Å		1.58 Å/pix.
x 288 pix.
= 455.04 Å		1.58 Å/pix.
x 288 pix.
= 455.04 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.58 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.045 / Movie #1: 0.045
Minimum - Maximum-0.09341251 - 0.20251693
Average (Standard dev.)0.00016793663 (±0.0032407593)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 455.04 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.581.581.58
M x/y/z288288288
origin x/y/z0.0000.0000.000
length x/y/z455.040455.040455.040
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS288288288
D min/max/mean-0.0930.2030.000

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Supplemental data

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Mask #1

Fileemd_12559_msk_1.map
Projections & Slices
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Half map: #2

Fileemd_12559_half_map_1.map
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Half map: #1

Fileemd_12559_half_map_2.map
Projections & Slices
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Sample components

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Entire : Substrate receptor scaffolding module of yeast Chelator-GID SR4 c...

EntireName: Substrate receptor scaffolding module of yeast Chelator-GID SR4 comprising Gid1, Gid4, Gid5, Gid8 and Gid9 bound to Fbp1
Components
  • Complex: Substrate receptor scaffolding module of yeast Chelator-GID SR4 comprising Gid1, Gid4, Gid5, Gid8 and Gid9 bound to Fbp1
    • Protein or peptide: Vacuolar import and degradation protein 28
    • Protein or peptide: Glucose-induced degradation protein 8
    • Protein or peptide: BJ4_G0018240.mRNA.1.CDS.1
    • Protein or peptide: Protein FYV10
    • Protein or peptide: Vacuolar import and degradation protein 24
    • Protein or peptide: Fructose-bisphosphatase

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Supramolecule #1: Substrate receptor scaffolding module of yeast Chelator-GID SR4 c...

SupramoleculeName: Substrate receptor scaffolding module of yeast Chelator-GID SR4 comprising Gid1, Gid4, Gid5, Gid8 and Gid9 bound to Fbp1
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Details: Generated by focused refinement of Chelator-GID SR4 + Fbp1 map
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 310 KDa

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Macromolecule #1: Vacuolar import and degradation protein 28

MacromoleculeName: Vacuolar import and degradation protein 28 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 105.609133 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MTVAYSLENL KKISNSLVGD QLAKVDYFLA PKCQIFQCLL SIEQSDGVEL KNAKLDLLYT LLHLEPQQRD IVGTYYFDIV SAIYKSMSL ASSFTKNNSS TNYKYIKLLN LCAGVYPNCG FPDLQYLQNG FIQLVNHKFL RSKCKIDEVV TIIELLKLFL L VDEKNCSD ...String:
MTVAYSLENL KKISNSLVGD QLAKVDYFLA PKCQIFQCLL SIEQSDGVEL KNAKLDLLYT LLHLEPQQRD IVGTYYFDIV SAIYKSMSL ASSFTKNNSS TNYKYIKLLN LCAGVYPNCG FPDLQYLQNG FIQLVNHKFL RSKCKIDEVV TIIELLKLFL L VDEKNCSD FNKSKFMEEE REVTETSHYQ DFKMAESLEH IIVKISSKYL DQISLKYIVR LKVSRPASPS SVKNDPFDNK GV DCTRAIP KKINISNMYD SSLLSLALLL YLRYHYMIPG DRKLRNDATF KMFVLGLLKS NDVNIRCVAL KFLLQPYFTE DKK WEDTRT LEKILPYLVK SFNYDPLPWW FDPFDMLDSL IVLYNEITPM NNPVLTTLAH TNVIFCILSR FAQCLSLPQH NEAT LKTTT KFIKICASFA ASDEKYRLLL LNDTLLLNHL EYGLESHITL IQDFISLKDE IKETTTESHS MCLPPIYDHD FVAAW LLLL KSFSRSVSAL RTTLKRNKIA QLLLQILSKT YTLTKECYFA GQDFMKPEIM IMGITLGSIC NFVVEFSNLQ SFMLRN GII DIIEKMLTDP LFNSKKAWDD NEDERRIALQ GIPVHEVKAN SLWVLRHLMY NCQNEEKFQL LAKIPMNLIL DFINDPC WA VQAQCFQLLR NLTCNSRKIV NILLEKFKDV EYKIDPQTGN KISIGSTYLF EFLAKKMRLL NPLDTQQKKA MEGILYII V NLAAVNENKK QLVIEQDEIL NIMSEILVET TTDSSSNGND SNLKLACLWV LNNLLWNSSV SHYTQYAIEN GLEPGHSPS DSENPQSTVT IGYNESVAGG YSRGKYYDEP DGDDSSSNAN DDEDDDNDEG DDEGDEFVRT PAAKGSTSNV QVTRATVERC RKLVEVGLY DLVRKNITDE SLSVREKART LLYHMDLLLK VK

UniProtKB: Vacuolar import and degradation protein 28

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Macromolecule #2: Glucose-induced degradation protein 8

MacromoleculeName: Glucose-induced degradation protein 8 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 55.803309 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MTISTLSNET TKSGSCSGQG KNGGKDFTYG KKCFTKEEWK EQVAKYSAMG ELYANKTIHY PLKIQPNSSG GSQDEGFATI QTTPIEPTL PRLLLNYFVS MAYEDSSIRM AKELGFIRNN KDIAVFNDLY KIKERFHIKH LIKLGRINEA MEEINSIFGL E VLEETFNA ...String:
MTISTLSNET TKSGSCSGQG KNGGKDFTYG KKCFTKEEWK EQVAKYSAMG ELYANKTIHY PLKIQPNSSG GSQDEGFATI QTTPIEPTL PRLLLNYFVS MAYEDSSIRM AKELGFIRNN KDIAVFNDLY KIKERFHIKH LIKLGRINEA MEEINSIFGL E VLEETFNA TGSYTGRTDR QQQQQQQQFD IDGDLHFKLL LLNLIEMIRS HHQQENITKD SNDFILNLIQ YSQNKLAIKA SS SVKKMQE LELAMTLLLF PLSDSADSGS IKLPKSLQNL YSISLRSKIA DLVNEKLLKF IHPRIQFEIS NNNSKFPDLL NSD KKIITQ NFTVYNNNLV NGSNGTKITH ISSDQPINEK MSSNEVTAAA NSVWLNQRDG NVGTGSAATT FHNLENKNYW NQTS ELLSS SNGKEKGLEF NNYYSSEFPY EPRLTQIMKL WCWCENQLHH NQIGVPRVEN SDENLYFQSG WSHPQFEKGG GSGGG SGGS AWSHPQFEK

UniProtKB: Glucose-induced degradation protein 8

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Macromolecule #3: BJ4_G0018240.mRNA.1.CDS.1

MacromoleculeName: BJ4_G0018240.mRNA.1.CDS.1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 108.28768 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSEYMDDVDR EFINCLFPSY LLQQPVAYDL WILYLQHRKL FHKLKNTNLI NADENPTGVG MGRTKLTALT RKEIWSKLMN LGVLGTISF EAVNDDYLIQ VYKYFYPDVN DFTLRFGVKD SNKNSVRVMK ASSDMRKNAQ ELLEPVLSER EMALNSNTSL E NDRNDDDD ...String:
MSEYMDDVDR EFINCLFPSY LLQQPVAYDL WILYLQHRKL FHKLKNTNLI NADENPTGVG MGRTKLTALT RKEIWSKLMN LGVLGTISF EAVNDDYLIQ VYKYFYPDVN DFTLRFGVKD SNKNSVRVMK ASSDMRKNAQ ELLEPVLSER EMALNSNTSL E NDRNDDDD DDDDDDDDDD DDDDDDDESD LESLEGEVDT DTDDNNEGDG SDNHEEGGEE GSRGADADVS SAQQRAERVA DP WIYQRSR SAINIETESR NLWDTSDKNS GLQYYPPDQS PSSSFSSPRV SSGNDKNDNE ATNVLSNSGS KKKNSMIPDI YKI LGYFLP SRWQAQPNNS LQLSQDGITH LQPNPDYHSY MTYERSSASS ASTRNRLRTS FENSGKVDFA VTWANKSLPD NKLT IFYYE IKVLSVTSTE SAENSNIVIG YKLVENELME ATTKKSVSRS SVAGSSSSLG GSNNMSSNRV PSTSFTMEGT QRRDY IYEG GVSAMSLNVD GSINKCQKYG FDLNVFGYCG FDGLITNSTE QSKEYAKPFG RDDVIGCGIN FIDGSIFFTK NGIHLG NAF TDLNDLEFVP YVALRPGNSI KTNFGLNEDF VFDIIGYQDK WKSLAYEHIC RGRQMDVSIE EFDSDESEED ETENGPE EN KSTNVNEDLM DIDQEDGAAG NKDTKKLNDE KDNNLKFLLG EDNRFIDGKL VRPDVNNINN LSVDDGSLPN TLNVMIND Y LIHEGLVDVA KGFLKDLQKD AVNVNGQHSE SKDVIRHNER QIMKEERMVK IRQELRYLIN KGQISKCINY IDNEIPDLL KNNLELVFEL KLANYLVMIK KSSSKDDDEI ENLILKGQEL SNEFIYDTKI PQSLRDRFSG QLSNVSALLA YSNPLVEAPK EISGYLSDE YLQERLFQVS NNTILTFLHK DSECALENVI SNTRAMLSTL LEYNAFGSTN SSDPRYYKAI NFDEDVLNL

UniProtKB: BJ4_G0038950.mRNA.1.CDS.1

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Macromolecule #4: Protein FYV10

MacromoleculeName: Protein FYV10 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 59.975102 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAEKSIFNEP DVDFHLKLNQ QLFHIPYELL SKRIKHTQAV INKETKSLHE HTAALNQIFE HNDVEHDELA LAKITEMIRK VDHIERFLN TQIKSYCQIL NRIKKRLEFF HELKDIKSQN SGTSHNGNNE GTRTKLIQWY QSYTNILIGD YLTRNNPIKY N SETKDHWN ...String:
MAEKSIFNEP DVDFHLKLNQ QLFHIPYELL SKRIKHTQAV INKETKSLHE HTAALNQIFE HNDVEHDELA LAKITEMIRK VDHIERFLN TQIKSYCQIL NRIKKRLEFF HELKDIKSQN SGTSHNGNNE GTRTKLIQWY QSYTNILIGD YLTRNNPIKY N SETKDHWN SGVVFLKQSQ LDDLIDYDVL LEANRISTSL LHERNLLPLI SWINENKKTL TKKSSILEFQ ARLQEYIELL KV DNYTDAI VCFQRFLLPF VKSNFTDLKL ASGLLIFIKY CNDQKPTSST SSGFDTEEIK SQSLPMKKDR IFQHFFHKSL PRI TSKPAV NTTDYDKSSL INLQSGDFER YLNLLDDQRW SVLNDLFLSD FYSMYGISQN DPLLIYLSLG ISSLKTRDCL HPSD DENGN QETETATTAE KEVEDLQLFT LHSLKRKNCP VCSETFKPIT QALPFAHHIQ SQLFENPILL PNGNVYDSKK LKKLA KTLK KQNLISLNPG QIMDPVDMKI FCESDSIKMY PT

UniProtKB: Protein FYV10

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Macromolecule #5: Vacuolar import and degradation protein 24

MacromoleculeName: Vacuolar import and degradation protein 24 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 41.291934 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MINNPKVDSV AEKPKAVTSK QSEQAASPEP TPAPPVSRNQ YPITFNLTST APFHLHDRHR YLQEQDLYKC ASRDSLSSLQ QLAHTPNGS TRKKYIVEDQ SPYSSENPVI VTSSYNHTVC TNYLRPRMQF TGYQISGYKR YQVTVNLKTV DLPKKDCTSL S PHLSGFLS ...String:
MINNPKVDSV AEKPKAVTSK QSEQAASPEP TPAPPVSRNQ YPITFNLTST APFHLHDRHR YLQEQDLYKC ASRDSLSSLQ QLAHTPNGS TRKKYIVEDQ SPYSSENPVI VTSSYNHTVC TNYLRPRMQF TGYQISGYKR YQVTVNLKTV DLPKKDCTSL S PHLSGFLS IRGLTNQHPE ISTYFEAYAV NHKELGFLSS SWKDEPVLNE FKATDQTDLE HWINFPSFRQ LFLMSQKNGL NS TDDNGTT NAAKKLPPQQ LPTTPSADAG NISRIFSQEK QFDNYLNERF IFMKWKEKFL VPDALLMEGV DGASYDGFYY IVH DQVTGN IQGFYYHQDA EKFQQLELVP SLKNKVESSD CSFEFA

UniProtKB: Vacuolar import and degradation protein 24

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Macromolecule #6: Fructose-bisphosphatase

MacromoleculeName: Fructose-bisphosphatase / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: fructose-bisphosphatase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 38.303473 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MPTLVNGPRR DSTEGFDTDI ITLPRFIIEH QKQFKNATGD FTLVLNALQF AFKFVSHTIR RAELVNLVGL AGASNFTGDQ QKKLDVLGD EIFINAMRAS GIIKVLVSEE QEDLIVFPTN TGSYAVCCDP IDGSSNLDAG VSVGTIASIF RLLPDSSGTI N DVLRCGKE ...String:
MPTLVNGPRR DSTEGFDTDI ITLPRFIIEH QKQFKNATGD FTLVLNALQF AFKFVSHTIR RAELVNLVGL AGASNFTGDQ QKKLDVLGD EIFINAMRAS GIIKVLVSEE QEDLIVFPTN TGSYAVCCDP IDGSSNLDAG VSVGTIASIF RLLPDSSGTI N DVLRCGKE MVAACYAMYG SSTHLVLTLG DGVDGFTLDT NLGEFILTHP NLRIPPQKAI YSINEGNTLY WNETIRTFIE KV KQPQADN NNKPFSARYV GSMVADVHRT FLYGGLFAYP CDKKSPNGKL RLLYEAFPMA FLMEQAGGKA VNDRGERILD LVP SHIHDK SSIWLGSSGE IDKFLDHIGK SQ

UniProtKB: Fructose-bisphosphatase

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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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 79.2 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

12557

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 74929
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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