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- EMDB-47949: Tubulin cofactors D,E,G bound to tubulin dimer -

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Basic information

Entry
Database: EMDB / ID: EMD-47949
TitleTubulin cofactors D,E,G bound to tubulin dimer
Map data
Sample
  • Complex: Tubulin cofactors D,E,G bound to tubulin dimer
    • Protein or peptide: Chromosome instability protein 1
    • Protein or peptide: GTP-binding protein CIN4
    • Protein or peptide: Tubulin alpha-1A chain
    • Protein or peptide: Tubulin beta chain
    • Protein or peptide: Designed ankyrin repeat protein -- Darpin
    • Protein or peptide: Protein PAC2
  • Ligand: GUANOSINE-5'-TRIPHOSPHATE
  • Ligand: GUANOSINE-5'-DIPHOSPHATE
KeywordsTubulin / cofactors / Tubulin cofactors / Tubulin biogenesis / Tubulin degradation / microtubules / CYTOSOLIC PROTEIN
Function / homology
Function and homology information


post-chaperonin tubulin folding pathway / tubulin complex assembly / motile cilium / alpha-tubulin binding / beta-tubulin binding / GTPase activator activity / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / protein folding ...post-chaperonin tubulin folding pathway / tubulin complex assembly / motile cilium / alpha-tubulin binding / beta-tubulin binding / GTPase activator activity / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / protein folding / mitotic cell cycle / microtubule cytoskeleton / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / hydrolase activity / GTPase activity / GTP binding / metal ion binding / cytoplasm
Similarity search - Function
: / Tubulin-specific chaperone D-like, ARM repeats / Tubulin-folding cofactor D / Tubulin-specific chaperone D-like, ARM repeat / ADP-ribosylation factor-like protein 2/3 / : / CAP-Gly domain signature. / CAP Gly-rich domain / CAP Gly-rich domain superfamily / CAP-Gly domain ...: / Tubulin-specific chaperone D-like, ARM repeats / Tubulin-folding cofactor D / Tubulin-specific chaperone D-like, ARM repeat / ADP-ribosylation factor-like protein 2/3 / : / CAP-Gly domain signature. / CAP Gly-rich domain / CAP Gly-rich domain superfamily / CAP-Gly domain / CAP-Gly domain profile. / CAP_GLY / Small GTPase Arf domain profile. / Sar1p-like members of the Ras-family of small GTPases / Small GTPase superfamily, ARF/SAR type / ADP-ribosylation factor family / ARF-like small GTPases; ARF, ADP-ribosylation factor / Leucine Rich repeat / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Small GTP-binding protein domain / Ubiquitin-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Tubulin alpha-1A chain / Tubulin beta chain / GTP-binding protein CIN4 / Protein PAC2 / Chromosome instability protein 1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Sus scrofa (pig) / Escherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsTaheri A / Al-bassam J
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: Nat Commun / Year: 2025
Title: Cryo-EM structures of the tubulin cofactors reveal the molecular basis of alpha/beta-tubulin biogenesis.
Authors: Aryan Taheri / Zhoaqian Wang / Bharti Singal / Fei Guo / Jawdat Al-Bassam /
Abstract: Microtubule polarity and dynamic polymerization arise from the self-association properties of the αβ-tubulin heterodimer. For decades, it has remained unclear how the tubulin cofactors TBCD, TBCE, ...Microtubule polarity and dynamic polymerization arise from the self-association properties of the αβ-tubulin heterodimer. For decades, it has remained unclear how the tubulin cofactors TBCD, TBCE, TBCC, and the Arl2 GTPase mediate the biogenesis of αβ-tubulin from individual α- and β-tubulins. Here, we use cryo-electron microscopy to determine structures of tubulin cofactors bound to αβ-tubulin. TBCD, TBCE, and Arl2 form a heterotrimeric cage-like assembly, we term TBC-DEG, around the αβ-tubulin heterodimer. The TBC-DEG-αβ-tubulin structures show that TBC-DEG wraps around β-tubulin while TBCE extends along α-tubulin. The TBC-DEG/TBCC-αβ-tubulin structures reveal that TBCC forms multi-domain interactions with Arl2 and TBCD to engage the αβ-tubulin intradimer-interface, promoting TBCE rotation while TBCD holds β-tubulin. TBCC engages the GTP-bound Arl2, multiple sites of TBCD, and the native αβ-tubulin intradimer interface near the α-tubulin N-site GTP. Together, these structures uncover transition states for αβ-tubulin biogenesis and degradation, suggesting a vise-like, GTP-hydrolysis-dependent mechanism in which TBCC binding to TBC-DEG modulates αβ-tubulin interfaces. Our studies provide structural evidence that tubulin cofactors act as enzymatic regulators that assemble the invariant αβ-tubulin architecture. By catalyzing α- and β-tubulin biogenesis and degradation, the TBC-DEG and TBCC assemblies regulate the polymerization competency of αβ-tubulin for microtubule formation.
History
DepositionNov 18, 2024-
Header (metadata) releaseFeb 4, 2026-
Map releaseFeb 4, 2026-
UpdateFeb 4, 2026-
Current statusFeb 4, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_47949.png

Downloads & links

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Map

FileDownload / File: emd_47949.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.32 Å/pix.
x 400 pix.
= 529.6 Å		1.32 Å/pix.
x 400 pix.
= 529.6 Å		1.32 Å/pix.
x 400 pix.
= 529.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.324 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0343
Minimum - Maximum-0.0017621794 - 1.9670148
Average (Standard dev.)0.0003521891 (±0.0142941065)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 529.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Tubulin cofactors D,E,G bound to tubulin dimer

EntireName: Tubulin cofactors D,E,G bound to tubulin dimer
Components
  • Complex: Tubulin cofactors D,E,G bound to tubulin dimer
    • Protein or peptide: Chromosome instability protein 1
    • Protein or peptide: GTP-binding protein CIN4
    • Protein or peptide: Tubulin alpha-1A chain
    • Protein or peptide: Tubulin beta chain
    • Protein or peptide: Designed ankyrin repeat protein -- Darpin
    • Protein or peptide: Protein PAC2
  • Ligand: GUANOSINE-5'-TRIPHOSPHATE
  • Ligand: GUANOSINE-5'-DIPHOSPHATE

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Supramolecule #1: Tubulin cofactors D,E,G bound to tubulin dimer

SupramoleculeName: Tubulin cofactors D,E,G bound to tubulin dimer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Macromolecule #1: Chromosome instability protein 1

MacromoleculeName: Chromosome instability protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 117.608211 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHHNNI RALLDSIQSG VQTVSPEKHQ QTIAAINKFQ DDPALLDTIL PRCVPLLTKS FFCMSQRDQK LVAELFYNLD KISHSKVLK SLDTSIFRLN EILNYLQDRA SPSSFSDVLC VYLNLSWLSV ILLSPYAFKD KFNKTLQVSS RFENYPICIP P INKIKAVL ...String:
MHHHHHHNNI RALLDSIQSG VQTVSPEKHQ QTIAAINKFQ DDPALLDTIL PRCVPLLTKS FFCMSQRDQK LVAELFYNLD KISHSKVLK SLDTSIFRLN EILNYLQDRA SPSSFSDVLC VYLNLSWLSV ILLSPYAFKD KFNKTLQVSS RFENYPICIP P INKIKAVL YFKNFTDAFD QLPEREQANV PFLNQFLKLF IQSSEKANYY FSNENLRHLQ QVALSNDGIK LLPKLFQISF NH GSHDILD AIVEFFHDHL SSNSTDTRFQ LAHSFAKIAK FLHQADPASF IELIDYTIEN TVSLLQAPCD SIDSNELHTS LLI IAEVAL AKILPIDLVD RVLTLIIPKT CHFQKSHFQI IKGHHIRDST NFIIWSVIRS NRSNSLSPQV LQSLLSHLLI NAFF DPELI IRYSSFAALQ ELLGRSNKSL ALNQNDIALI LQANWKDLPR SFEENSGLIR RLFNPENTSK SAVCVWKVFR DWSFN WNLL ENLHLTTMKL NIDYNLVPLI KSKLSSPALL QEVLNKAGSS VTQNCQILYL YLKLFENDVN CPKISEICID IYQKKI KFQ LTTQAKRQFN DNSPELFQIF VILKYWQLTG QNDFNQELFW KFVDIVSPQK KLNLYNEFIP IIQQIISQCV SLNYTRI VQ LIKSDNELTC RSICHMPDQE KMCSLFFSQF PLLSPQSRSL LIGELDHHWD VRISLLPSNS YRKFRNIIIN CLDDYTIT Q QGDVGRLVRI QALKLMQSHP DFLSGDCDSI NPKLTRLLAE PVPEIRKLSY QLLASATSQI TVLSDSSILN FRHKQGLSE EFWKGYAVSA GAIHFTDSQL TSSIDSFIVY YRSLSPSQQL ELCHDLIRII PSAKQIAESR IRDRNKDPLT GGMRFDTIKF TIHCVKFWT RIMESGLVVL HPNFNFQGVF AKFYNLHLLD CTTLRVSVIK FFPFLAISCY HTMRENADQK NLSNIILKRL L VLVKREYA ATKSKFMTDQ NVALQGMFQI FLELGVTRQL QALQVACQKH ELANILESDI TL

UniProtKB: Chromosome instability protein 1

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Macromolecule #2: GTP-binding protein CIN4

MacromoleculeName: GTP-binding protein CIN4 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 22.096717 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGLLSIIRKQ KLRDKEIRCL ILGLDNSGKS TIVNKLLPKD EQNNDGIMPT VGFQIHSLMI KDVTISLWDI GGQRTLRPFW DNYFDKTQA MIWCIDVSLS MRFDETLQEL KELINRDENR IGYECAVIVV LNKIDLVEDK SELHRRCLLV ESELKCLFKP D IRIELVKC SGVTGEGIDN LRDRLVESCH FTQ

UniProtKB: GTP-binding protein CIN4

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Macromolecule #3: Tubulin alpha-1A chain

MacromoleculeName: Tubulin alpha-1A chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 50.121266 KDa
SequenceString: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFSVFH SFGGGTGSGF TSLLMERLSV D YGKKSKLE ...String:
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFSVFH SFGGGTGSGF TSLLMERLSV D YGKKSKLE FSIYPAPQVS TAVVEPYNSI LTTHTTLEHS DCAFMVDNEA IYDICRRNLD IERPTYTNLN RLIGQIVSSI TA SLRFDGA LNVDLTEFQT NLVPYPRAHF PLATYAPVIS AEKAYHEQLS VAEITNACFE PANQMVKCDP RHGKYMACCL LYR GDVVPK DVNAAIATIK TKRTIQFVDW CPTGFKVGIN YEPPTVVPGG DLAKVQRAVC MLSNTTAIAE AWARLDHKFD LMYA KRAFV HWYVGEGMEE GEFSEAREDM AALEKDYEEV GVDSVEGEGE EEGEEY

UniProtKB: Tubulin alpha-1A chain

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Macromolecule #4: Tubulin beta chain

MacromoleculeName: Tubulin beta chain / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 49.90777 KDa
SequenceString: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKESESCDC LQGFQLTHSL GGGTGSGMGT LLISKIREEY P DRIMNTFS ...String:
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKESESCDC LQGFQLTHSL GGGTGSGMGT LLISKIREEY P DRIMNTFS VVPSPKVSDT VVEPYNATLS VHQLVENTDE TYCIDNEALY DICFRTLKLT TPTYGDLNHL VSATMSGVTT CL RFPGQLN ADLRKLAVNM VPFPRLHFFM PGFAPLTSRG SQQYRALTVP ELTQQMFDAK NMMAACDPRH GRYLTVAAVF RGR MSMKEV DEQMLNVQNK NSSYFVEWIP NNVKTAVCDI PPRGLKMSAT FIGNSTAIQE LFKRISEQFT AMFRRKAFLH WYTG EGMDE MEFTEAESNM NDLVSEYQQY QDATADEQGE FEEEGEEDEA

UniProtKB: Tubulin beta chain

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Macromolecule #5: Designed ankyrin repeat protein -- Darpin

MacromoleculeName: Designed ankyrin repeat protein -- Darpin / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 17.955262 KDa
SequenceString:
MRGSHHHHHH GSDLGKKLLE AARAGQDDEV RVLMANGADV NATDASGLTP LHLAATYGHL EIVEVLLKHG ADVSASDLMG STPLHLAAL IGHLEIVEVL LKHGADVNAV DTWGDTPLRL AAVMGHLKIV EALLKHGADV NAQDKFGKTA YDTSIDNGSE D LAEILQKL N

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Macromolecule #6: Protein PAC2

MacromoleculeName: Protein PAC2 / type: protein_or_peptide / ID: 6
Details: Chain E contains a well-resolved C-terminal region that was modeled with full side-chain identities. Density for the LRR and CAP-Gly domains is weaker and discontinuous, consistent with ...Details: Chain E contains a well-resolved C-terminal region that was modeled with full side-chain identities. Density for the LRR and CAP-Gly domains is weaker and discontinuous, consistent with flexibility of this portion of the protein in the complex. Therefore, residues in these regions are modeled as poly-alanine to represent the backbone trace and overall topology only (listed as UNK in the entry). Side-chain identities are not asserted in these low-density regions. The sequence register is anchored by the well-resolved C-terminal domain and supported by the AlphaFold prediction.
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 41.916664 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...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)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)QSLVLK IKIRAGKKPS SDLDYWVLPS FTVR YVKSV ICRKLNFDIL NVKLFHENSE GMINEIKYNF RPISDFNVVN GDIIHVSSPV NNKSIQKVNS PS

UniProtKB: Protein PAC2

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Macromolecule #7: GUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 2 / Formula: GTP
Molecular weightTheoretical: 523.18 Da
Chemical component information

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

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Macromolecule #8: GUANOSINE-5'-DIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 8 / Number of copies: 1 / Formula: GDP
Molecular weightTheoretical: 443.201 Da
Chemical component information

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

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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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K2 BASE (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.1 µm / Nominal defocus min: 0.9 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: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 275487
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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