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- EMDB-32465: Subcomplexes A and E in NDH complex from Arabidopsis -

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Basic information

Entry
Database: EMDB / ID: EMD-32465
TitleSubcomplexes A and E in NDH complex from Arabidopsis
Map data
Sample
  • Complex: Subcomplex A and E in NDH complex from Arabidopsis
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit L, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit M, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic
    • Protein or peptide: NdhO
    • Protein or peptide: NdhT
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster
Function / homology
Function and homology information


NAD(P)H dehydrogenase complex (plastoquinone) / NADH dehydrogenase complex (plastoquinone) assembly / cellular response to sulfate starvation / thylakoid membrane / chloroplast thylakoid / NADPH dehydrogenase activity / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / chloroplast envelope / photosynthetic electron transport in photosystem I / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor ...NAD(P)H dehydrogenase complex (plastoquinone) / NADH dehydrogenase complex (plastoquinone) assembly / cellular response to sulfate starvation / thylakoid membrane / chloroplast thylakoid / NADPH dehydrogenase activity / Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions / chloroplast envelope / photosynthetic electron transport in photosystem I / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / electron transport coupled proton transport / plastid / chloroplast stroma / chloroplast thylakoid membrane / photosynthesis, light reaction / NADH dehydrogenase (ubiquinone) activity / quinone binding / defense response to fungus / aerobic respiration / photosynthesis / chloroplast / NAD binding / 4 iron, 4 sulfur cluster binding / membrane => GO:0016020 / iron ion binding / plasma membrane
Similarity search - Function
NAD(P)H-quinone oxidoreductase subunit O / Cyanobacterial and plant NDH-1 subunit O / NAD(P)H-quinone oxidoreductase subunit M / NAD(P)H-quinone oxidoreductase subunit L / NAD(P)H-quinone oxidoreductase, subunit N / Cyanobacterial and plastid NDH-1 subunit M / NADH dehydrogenase transmembrane subunit / NADH-quinone oxidoreductase cyanobacterial subunit N / NADH-plastoquinone oxidoreductase, subunit I / 4Fe-4S dicluster domain ...NAD(P)H-quinone oxidoreductase subunit O / Cyanobacterial and plant NDH-1 subunit O / NAD(P)H-quinone oxidoreductase subunit M / NAD(P)H-quinone oxidoreductase subunit L / NAD(P)H-quinone oxidoreductase, subunit N / Cyanobacterial and plastid NDH-1 subunit M / NADH dehydrogenase transmembrane subunit / NADH-quinone oxidoreductase cyanobacterial subunit N / NADH-plastoquinone oxidoreductase, subunit I / 4Fe-4S dicluster domain / Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. / NADH-ubiquinone oxidoreductase, 20 Kd subunit / NADH-quinone oxidoreductase, chain I / NAD(P)H-quinone oxidoreductase subunit D/H / NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 49 Kd subunit signature. / NADH-quinone oxidoreductase, subunit D / Respiratory-chain NADH dehydrogenase, 49 Kd subunit / NADH dehydrogenase, subunit C / NADH:ubiquinone oxidoreductase, 30kDa subunit, conserved site / Respiratory chain NADH dehydrogenase 30 Kd subunit signature. / NADH:ubiquinone oxidoreductase, 30kDa subunit / NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily / Respiratory-chain NADH dehydrogenase, 30 Kd subunit / NADH:ubiquinone oxidoreductase-like, 20kDa subunit / NADH ubiquinone oxidoreductase, 20 Kd subunit / [NiFe]-hydrogenase, large subunit / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain
Similarity search - Domain/homology
NdhO / NAD(P)H-quinone oxidoreductase subunit H, chloroplastic / NAD(P)H-quinone oxidoreductase subunit J, chloroplastic / NAD(P)H-quinone oxidoreductase subunit I, chloroplastic / NAD(P)H-quinone oxidoreductase subunit K, chloroplastic / NAD(P)H-quinone oxidoreductase subunit M, chloroplastic / NAD(P)H-quinone oxidoreductase subunit L, chloroplastic / NAD(P)H-quinone oxidoreductase subunit N, chloroplastic
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress) / thale cress (thale cress)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.33 Å
AuthorsPan XW / Li M
Funding support China, 5 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2017YFA0503702 China
Chinese Academy of SciencesXDB27020106 China
National Natural Science Foundation of China (NSFC)31770778 China
National Natural Science Foundation of China (NSFC)31930064 China
National Natural Science Foundation of China (NSFC)31970264 China
CitationJournal: Mol Plant / Year: 2022
Title: Supramolecular assembly of chloroplast NADH dehydrogenase-like complex with photosystem I from Arabidopsis thaliana.
Authors: Xiaodong Su / Duanfang Cao / Xiaowei Pan / Lifang Shi / Zhenfeng Liu / Luca Dall'Osto / Roberto Bassi / Xinzheng Zhang / Mei Li /
Abstract: Cyclic electron transport/flow (CET/CEF) in chloroplasts is a regulatory process essential for the optimization of plant photosynthetic efficiency. A crucial CEF pathway is catalyzed by a membrane- ...Cyclic electron transport/flow (CET/CEF) in chloroplasts is a regulatory process essential for the optimization of plant photosynthetic efficiency. A crucial CEF pathway is catalyzed by a membrane-embedded NADH dehydrogenase-like (NDH) complex that contains at least 29 protein subunits and associates with photosystem I (PSI) to form the NDH-PSI supercomplex. Here, we report the 3.9 Å resolution structure of the Arabidopsis thaliana NDH-PSI (AtNDH-PSI) supercomplex. We constructed structural models for 26 AtNDH subunits, among which 11 are unique to chloroplasts and stabilize the core part of the NDH complex. In the supercomplex, one NDH can bind up to two PSI-light-harvesting complex I (PSI-LHCI) complexes at both sides of its membrane arm. Two minor LHCIs, Lhca5 and Lhca6, each present in one PSI-LHCI, interact with NDH and contribute to supercomplex formation and stabilization. Collectively, our study reveals the structural details of the AtNDH-PSI supercomplex assembly and provides a molecular basis for further investigation of the regulatory mechanism of CEF in plants.
History
DepositionDec 26, 2021-
Header (metadata) releaseMar 16, 2022-
Map releaseMar 16, 2022-
UpdateMar 16, 2022-
Current statusMar 16, 2022Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.025
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  • Surface level: 0.025
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  • Surface view with fitted model
  • Atomic models: PDB-7wfg
  • Surface level: 0.025
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7wfg
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_32465.png

Downloads & links

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Map

FileDownload / File: emd_32465.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.04 Å
Density
Contour LevelBy AUTHOR: 0.02 / Movie #1: 0.025
Minimum - Maximum-0.026721116 - 0.123644345
Average (Standard dev.)0.00014574431 (±0.0020968139)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-200-200-200
Dimensions400400400
Spacing400400400
CellA=B=C: 416.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.041.041.04
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z416.000416.000416.000
α/β/γ90.00090.00090.000
start NX/NY/NZ139118109
NX/NY/NZ123164187
MAP C/R/S123
start NC/NR/NS-200-200-200
NC/NR/NS400400400
D min/max/mean-0.0270.1240.000

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Supplemental data

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Sample components

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Entire : Subcomplex A and E in NDH complex from Arabidopsis

EntireName: Subcomplex A and E in NDH complex from Arabidopsis
Components
  • Complex: Subcomplex A and E in NDH complex from Arabidopsis
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit L, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit M, chloroplastic
    • Protein or peptide: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic
    • Protein or peptide: NdhO
    • Protein or peptide: NdhT
  • Ligand: IRON/SULFUR CLUSTERIron–sulfur cluster

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Supramolecule #1: Subcomplex A and E in NDH complex from Arabidopsis

SupramoleculeName: Subcomplex A and E in NDH complex from Arabidopsis / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Arabidopsis thaliana (thale cress)

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Macromolecule #1: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit H, chloroplastic
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 45.553637 KDa
SequenceString: MKRPVTGKDL MIVNMGPHHP SMHGVLRLIV TLDGEDVVDC EPILGYLHRG MEKIAENRAI IQYLPYVTRW DYLATMFTEA ITVNGPEQL GNIQVPKRAS YIRVIMLELS RIASHLLWLG PFMADIGAQT PFFYIFRERE FVYDLFEAAT GMRMMHNFFR I GGIAADLP ...String:
MKRPVTGKDL MIVNMGPHHP SMHGVLRLIV TLDGEDVVDC EPILGYLHRG MEKIAENRAI IQYLPYVTRW DYLATMFTEA ITVNGPEQL GNIQVPKRAS YIRVIMLELS RIASHLLWLG PFMADIGAQT PFFYIFRERE FVYDLFEAAT GMRMMHNFFR I GGIAADLP YGWIDKCLDF CDYFLTEVVE YQKLITRNPI FLERVEGVGI IGGEEAINWG LSGPMLRASG IPWDLRKIDR YE SYDEFEW EIQWQKQGDS LARYLVRLSE MTESIKIIQQ ALEGLPGGPY ENLESRGFDR KRNPEWNDFE YRFISKKPSP TFE LSKQEL YVRVEAPKGE LGIFLIGDQS GFPWRWKIRP PGFINLQILP ELVKRMKLAD IMTILGSIDI IMGEVDR

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Macromolecule #2: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 20.107314 KDa
SequenceString:
MLPMITGFMN YGQQTLRAAR YIGQGFMITL SHTNRLPVTI QYPYEKLITS ERFRGRIHFE FDKCIACEVC VRVCPIDLPV VDWKLETNI RKKRLLNYSI DFGICIFCGN CVEYCPTNCL SMTEEYEFST YDRHELNYNQ IALGRLPMSV IDDYTIRTIW N SPQTKNGV NPLI

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Macromolecule #3: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic
type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 18.57916 KDa
SequenceString:
MQGTLSVWLA KRGLVHRSLG FDYQGIETLQ IKPEDWHSIA VILYVYGYNY LRSQCAYDVA PGGLLASVYH LTRIEYGVNQ AEEVCIKVF THRSNPRIPS VFWVWKSTDF QERESYDMLG ITYDSHPRLK RILMPESWIG WPLRKDYIAP NFYEIQDAY

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Macromolecule #4: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 25.39627 KDa
SequenceString: MNSIKFPILD RTTKNSVIST TLNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR YGLVPRSSPR QADLILTAGT VTMKMAPSL VRLYEQMPEP KYVIAMGACT ITGGMFSTDS YSTVRGVDKL IPVDVYLPGC PPKPEAVIDA ITKLRKKIAR E IYKDRIRP ...String:
MNSIKFPILD RTTKNSVIST TLNDLSNWSR LSSLWPLLYG TSCCFIEFAS LIGSRFDFDR YGLVPRSSPR QADLILTAGT VTMKMAPSL VRLYEQMPEP KYVIAMGACT ITGGMFSTDS YSTVRGVDKL IPVDVYLPGC PPKPEAVIDA ITKLRKKIAR E IYKDRIRP QQGNRCFTTN HKFFVVRSPH IGNYDQELLY PPSSTSEIST ETFFKYKSPV SSHELVN

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Macromolecule #5: NAD(P)H-quinone oxidoreductase subunit L, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit L, chloroplastic
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 21.98785 KDa
SequenceString:
MSRCGSLGLY APNALPSLSL KPRSVKSPFC ITSHTKPNDT LLHNVNKMRA KACDILGAKK TILAAQLGAV LATIDHPALA ITGVNNQQE LSSVVLDIGI ISVWYFLVMP PIIMNWLRVR WYRRKFFEMY LQFMFVFMFF PGLLLWAPFL NFRKFPRDPN M KNPWDKPT DPDSIKNVYL KYPYATPEDY DLD

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Macromolecule #6: NAD(P)H-quinone oxidoreductase subunit M, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit M, chloroplastic
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 24.820828 KDa
SequenceString: MVAAFSYTAC TKLSLLHPSM VAQIRPRTTQ KAFVVTNPEQ DSTLEVQETE TLKEEQSTEK MKKQPTPLRP VEKQLNVKSK GMGDFGGQW LSSVTRHVRI YAAYIDPETC EFDQSQMDKL TLILDPTEEF VWDDESCNKV YSYFQELVDH YEGAPLTEYT L RLIGSDVE ...String:
MVAAFSYTAC TKLSLLHPSM VAQIRPRTTQ KAFVVTNPEQ DSTLEVQETE TLKEEQSTEK MKKQPTPLRP VEKQLNVKSK GMGDFGGQW LSSVTRHVRI YAAYIDPETC EFDQSQMDKL TLILDPTEEF VWDDESCNKV YSYFQELVDH YEGAPLTEYT L RLIGSDVE HYIRKMLFDG EIQYNMDARV LNFSMGKPRV QFNTSNIEGG GDGQPQEDA

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Macromolecule #7: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic

MacromoleculeName: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
EC number: Translocases; Catalysing the translocation of protons; Linked to oxidoreductase reactions
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 23.430254 KDa
SequenceString: MGSRAICIQR VAPPCFEASQ VKKIKTVGSF LVNTRSKRRR STGVKCSSIA DYIGGDLVKP DIGQWLQDVE EHKAIAIYAP HEGGYEGRY LNRLKMQGYY FLDISARGLG DPETTLLKNY PVCPAHLGKQ PIARWYYPPE VDYRLAALPP SAKGLVVWVL E AKVLSKSE ...String:
MGSRAICIQR VAPPCFEASQ VKKIKTVGSF LVNTRSKRRR STGVKCSSIA DYIGGDLVKP DIGQWLQDVE EHKAIAIYAP HEGGYEGRY LNRLKMQGYY FLDISARGLG DPETTLLKNY PVCPAHLGKQ PIARWYYPPE VDYRLAALPP SAKGLVVWVL E AKVLSKSE LQFLALLPSL RPNVRVIAEC GNWRKFVWKP LAEIANLAAQ E

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Macromolecule #8: NdhO

MacromoleculeName: NdhO / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 17.679381 KDa
SequenceString:
MAFSATLSQL SSLSTISSSL PISSRRLPHR SLPQFTVKAE AEKEKQSAQA KSDGEASPAA TKTPKTLPKK PVYSMKKGQI VRVEKEKYL NSINYLSVGH PPFYKGLDYI YEDRGEVLDL RVFETGEYAL VGWVGIPTAP AWLPTDMLIK CEKLVYERM

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Macromolecule #9: NdhT

MacromoleculeName: NdhT / type: protein_or_peptide / ID: 9
Details: All Residues in NdhT were modeled as UNK. The real sequence of the entity is: ...Details: All Residues in NdhT were modeled as UNK. The real sequence of the entity is: MAYATSTYARTSCIILPKIQNGAHFTDNTKAFRRITARRVTRISSQGPTKPPKPSPGVDTRIHWESPDEGWIGGRSDPAKSVDEDKTNLLSDEKFAELIKDSFDSHYQFLGVSTDAHLEEIKSAYRRLSKEYHPDTTSLPLKTASEKFMKLREVYNVLSDEETRRFYDWTLAQEVASRQAEKMRMKLEDPKEQDFRGYESIPDMVDRLGGRNMELSDQAMTALTFDILIVLFAVCCIVFVIVFKDPSY
Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: thale cress (thale cress)
Molecular weightTheoretical: 10.400812 KDa
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)

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Macromolecule #10: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 10 / Number of copies: 3 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

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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: 7.8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 60.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6khj

Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.33 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 76085

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