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- EMDB-37477: Structure of human phagocyte NADPH oxidase in the activated state -

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Basic information

Entry
Database: EMDB / ID: EMD-37477
TitleStructure of human phagocyte NADPH oxidase in the activated state
Map datacomposite map after focused refinement
Sample
  • Complex: activated NOX2-p22 complex
    • Protein or peptide: x 7 types
  • Ligand: x 7 types
KeywordsNOX2 / p22 / CYBA / CYBB / TP1170 / NOX / p67 / Rac / p47 / OXIDOREDUCTASE
Function / homology
Function and homology information


smooth muscle hypertrophy / reactive oxygen species biosynthetic process / cellular response to L-glutamine / regulation of respiratory burst involved in inflammatory response / positive regulation of toll-like receptor 2 signaling pathway / hypoxia-inducible factor-1alpha signaling pathway / superoxide-generating NADPH oxidase activator activity / phagolysosome / superoxide-generating NAD(P)H oxidase activity / positive regulation of epidermal growth factor-activated receptor activity ...smooth muscle hypertrophy / reactive oxygen species biosynthetic process / cellular response to L-glutamine / regulation of respiratory burst involved in inflammatory response / positive regulation of toll-like receptor 2 signaling pathway / hypoxia-inducible factor-1alpha signaling pathway / superoxide-generating NADPH oxidase activator activity / phagolysosome / superoxide-generating NAD(P)H oxidase activity / positive regulation of epidermal growth factor-activated receptor activity / positive regulation of defense response to bacterium / mucus secretion / Cross-presentation of particulate exogenous antigens (phagosomes) / perinuclear endoplasmic reticulum / cytochrome complex assembly / NADPH oxidase complex / WNT5:FZD7-mediated leishmania damping / respiratory burst / cellular response to testosterone stimulus / regulation of release of sequestered calcium ion into cytosol / ROS and RNS production in phagocytes / phosphatidylinositol-3,4-bisphosphate binding / cellular response to ethanol / Oxidoreductases / superoxide anion generation / response to angiotensin / hydrogen peroxide biosynthetic process / protein targeting to membrane / positive regulation of mucus secretion / positive regulation of p38MAPK cascade / positive regulation of reactive oxygen species biosynthetic process / monoatomic ion channel complex / response to aldosterone / small GTPase-mediated signal transduction / superoxide metabolic process / Detoxification of Reactive Oxygen Species / tertiary granule membrane / RHO GTPases Activate NADPH Oxidases / RAC2 GTPase cycle / RAC3 GTPase cycle / cellular defense response / specific granule membrane / positive regulation of phagocytosis / monoatomic ion transmembrane transport / RAC1 GTPase cycle / cellular response to cadmium ion / phosphatidylinositol binding / response to nutrient / secretory granule / establishment of localization in cell / cellular response to glucose stimulus / positive regulation of JNK cascade / cytoplasmic side of plasma membrane / defense response / VEGFA-VEGFR2 Pathway / cellular response to reactive oxygen species / SH3 domain binding / phagocytic vesicle membrane / positive regulation of angiogenesis / positive regulation of interleukin-6 production / positive regulation of tumor necrosis factor production / nuclear envelope / flavin adenine dinucleotide binding / oxidoreductase activity / electron transfer activity / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / endosome / response to xenobiotic stimulus / inflammatory response / protein heterodimerization activity / innate immune response / GTPase activity / neuronal cell body / dendrite / heme binding / Neutrophil degranulation / endoplasmic reticulum membrane / GTP binding / positive regulation of DNA-templated transcription / membrane / metal ion binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Cytochrome b245, heavy chain / Cytochrome b558 alpha-subunit / Cytochrome Cytochrome b558 alpha-subunit / Neutrophil cytosol factor 1 / Neutrophil cytosol factor 1, C-terminal / Neutrophil cytosol factor 1, PBR/AIR / Neutrophil cytosol factor 1, PX domain / Neutrophil cytosol factor 1, first SH3 domain / Neutrophil cytosol factor 1, second SH3 domain / NADPH oxidase subunit p47Phox, C terminal domain ...Cytochrome b245, heavy chain / Cytochrome b558 alpha-subunit / Cytochrome Cytochrome b558 alpha-subunit / Neutrophil cytosol factor 1 / Neutrophil cytosol factor 1, C-terminal / Neutrophil cytosol factor 1, PBR/AIR / Neutrophil cytosol factor 1, PX domain / Neutrophil cytosol factor 1, first SH3 domain / Neutrophil cytosol factor 1, second SH3 domain / NADPH oxidase subunit p47Phox, C terminal domain / Neutrophil cytosol factor 1, PBR/AIR / Ferric reductase, NAD binding domain / Ferric reductase NAD binding domain / FAD-binding 8 / FAD-binding domain / Ferric reductase transmembrane component-like domain / Ferric reductase like transmembrane component / PhoX homologous domain, present in p47phox and p40phox. / PX domain profile. / PX domain / Phox homology / PX domain superfamily / small GTPase Rab1 family profile. / Small GTPase Rho / small GTPase Rho family profile. / small GTPase Ras family profile. / FAD-binding domain, ferredoxin reductase-type / Ferredoxin-NADP reductase (FNR), nucleotide-binding domain / Ferredoxin reductase-type FAD binding domain profile. / Riboflavin synthase-like beta-barrel / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / SH3 domain / Small GTPase / Ras family / Rab subfamily of small GTPases / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Small GTP-binding protein domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
: / Rac family small GTPase 1 / Cytochrome b-245 heavy chain / Cytochrome b-245 light chain / Neutrophil cytosol factor 1
Similarity search - Component
Biological speciesHomo sapiens (human) / Mus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.79 Å
AuthorsChen L / Liu X
Funding support China, 3 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31821091 China
Ministry of Science and Technology (MoST, China)2022YFA1303000 China
National Natural Science Foundation of China (NSFC)32225027 China
CitationJournal: Nature / Year: 2024
Title: Structure of human phagocyte NADPH oxidase in the activated state.
Authors: Xiaoyu Liu / Yiting Shi / Rui Liu / Kangcheng Song / Lei Chen /
Abstract: Phagocyte NADPH oxidase, a protein complex with a core made up of NOX2 and p22 subunits, is responsible for transferring electrons from intracellular NADPH to extracellular oxygen. This process ...Phagocyte NADPH oxidase, a protein complex with a core made up of NOX2 and p22 subunits, is responsible for transferring electrons from intracellular NADPH to extracellular oxygen. This process generates superoxide anions that are vital for killing pathogens. The activation of phagocyte NADPH oxidase requires membrane translocation and the binding of several cytosolic factors. However, the exact mechanism by which cytosolic factors bind to and activate NOX2 is not well understood. Here we present the structure of the human NOX2-p22 complex activated by fragments of three cytosolic factors: p47, p67 and Rac1. The structure reveals that the p67-Rac1 complex clamps onto the dehydrogenase domain of NOX2 and induces its contraction, which stabilizes the binding of NADPH and results in a reduction of the distance between the NADPH-binding domain and the flavin adenine dinucleotide (FAD)-binding domain. Furthermore, the dehydrogenase domain docks onto the bottom of the transmembrane domain of NOX2, which reduces the distance between FAD and the inner haem. These structural rearrangements might facilitate the efficient transfer of electrons between the redox centres in NOX2 and lead to the activation of phagocyte NADPH oxidase.
History
DepositionSep 18, 2023-
Header (metadata) releaseJan 24, 2024-
Map releaseJan 24, 2024-
UpdateMar 20, 2024-
Current statusMar 20, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_37477.png

Downloads & links

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Map

FileDownload / File: emd_37477.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationcomposite map after focused refinement
Voxel sizeX=Y=Z: 1.028 Å
Density
Contour LevelBy AUTHOR: 0.55
Minimum - Maximum-3.3479059 - 7.1146994
Average (Standard dev.)0.01625477 (±0.08593273)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 328.96 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_37477_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map of consensus refinement

Fileemd_37477_half_map_1.map
Annotationhalf map of consensus refinement
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map of consensus refinement

Fileemd_37477_half_map_2.map
Annotationhalf map of consensus refinement
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : activated NOX2-p22 complex

EntireName: activated NOX2-p22 complex
Components
  • Complex: activated NOX2-p22 complex
    • Protein or peptide: Cytochrome b-245 light chain
    • Protein or peptide: Cytochrome b-245 heavy chain
    • Protein or peptide: Neutrophil cytosol factor 1
    • Protein or peptide: Neutrophil cytosolic factor 2 (65kDa, chronic granulomatous disease, autosomal 2), isoform CRA_a
    • Protein or peptide: Rac family small GTPase 1
    • Protein or peptide: 7D5 Fab heavy chain
    • Protein or peptide: 7D5 Fab light chain
  • Ligand: PROTOPORPHYRIN IX CONTAINING FE
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: MAGNESIUM ION
  • Ligand: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
  • Ligand: DIHYDROFLAVINE-ADENINE DINUCLEOTIDE
  • Ligand: GUANOSINE-5'-TRIPHOSPHATE
  • Ligand: water

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Supramolecule #1: activated NOX2-p22 complex

SupramoleculeName: activated NOX2-p22 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Cytochrome b-245 light chain

MacromoleculeName: Cytochrome b-245 light chain / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.005398 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIVAGVFVC LLEYPRGKRK KGSTMERWGQ KYMTAVVKLF GPFTRNYYV RAVLHLLLSV PAGFLLATIL GTACLAIASG IYLLAAVRGE QWTPIEPKPR ERPQIGGTIK QPPSNPPPRP P AEARKKPS ...String:
MGQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIVAGVFVC LLEYPRGKRK KGSTMERWGQ KYMTAVVKLF GPFTRNYYV RAVLHLLLSV PAGFLLATIL GTACLAIASG IYLLAAVRGE QWTPIEPKPR ERPQIGGTIK QPPSNPPPRP P AEARKKPS EEEAAAAAGG PPGGPQVNPI PVTDEVV

UniProtKB: Cytochrome b-245 light chain

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Macromolecule #2: Cytochrome b-245 heavy chain

MacromoleculeName: Cytochrome b-245 heavy chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 65.412727 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGNWAVNEGL SIFVILVWLG LNVFLFVWYY RVYDIPPKFF YTRKLLGSAL ALARAPAACL NFNCMLILLP VCRNLLSFLR GSSACCSTR VRRQLDRNLT FHKMVAWMIA LHSAIHTIAH LFNVEWCVNA RVNNSDPYSV ALSELGDRQN ESYLNFARKR I KNPEGGLY ...String:
MGNWAVNEGL SIFVILVWLG LNVFLFVWYY RVYDIPPKFF YTRKLLGSAL ALARAPAACL NFNCMLILLP VCRNLLSFLR GSSACCSTR VRRQLDRNLT FHKMVAWMIA LHSAIHTIAH LFNVEWCVNA RVNNSDPYSV ALSELGDRQN ESYLNFARKR I KNPEGGLY LAVTLLAGIT GVVITLCLIL IITSSTKTIR RSYFEVFWYT HHLFVIFFIG LAIHGAERIV RGQTAESLAV HN ITVCEQK ISEWGKIKEC PIPQFAGNPP MTWKWIVGPM FLYLCERLVR FWRSQQKVVI TKVVTHPFKT IELQMKKKGF KME VGQYIF VKCPKVSKLE WHPFTLTSAP EEDFFSIHIR IVGDWTEGLF NACGCDKQEF QDAWKLPKIA VDGPFGTASE DVFS YEVVM LVGAGIGVTP FASILKSVWY KYCNNATNLK LKKIYFYWLC RDTHAFEWFA DLLQLLESQM QERNNAGFLS YNIYL TGWD ESQANHFAVH HDEEKDVITG LKQKTLYGRP NWDNEFKTIA SQHPNTRIGV FLCGPEALAE TLSKQSISNS ESGPRG VHF IFNKENF

UniProtKB: Cytochrome b-245 heavy chain

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Macromolecule #3: Neutrophil cytosol factor 1

MacromoleculeName: Neutrophil cytosol factor 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 32.813297 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAEN RQGTLTEYCS TLMSLPTKIS RCPHLLDFFK VRPDDLKLPT DNQTKKPETY LMPKDGKSTA TDITGPIILQ T YRAIANYE ...String:
MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAEN RQGTLTEYCS TLMSLPTKIS RCPHLLDFFK VRPDDLKLPT DNQTKKPETY LMPKDGKSTA TDITGPIILQ T YRAIANYE KTSGSEMALS TGDVVEVVEK SESGWWFCQM KAKRGWIPAS FLEPLDSPDE TEDPEPNYAG EPYVAIKAYT AV EGDEVSL LEGEAVEVIH KLLDGWWVIR KDDVTGYFPS MYLQKSGQD

UniProtKB: Neutrophil cytosol factor 1

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Macromolecule #4: Neutrophil cytosolic factor 2 (65kDa, chronic granulomatous disea...

MacromoleculeName: Neutrophil cytosolic factor 2 (65kDa, chronic granulomatous disease, autosomal 2), isoform CRA_a
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.978535 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSLVEAISLW NEGVLAADKK DWKGALDAFS AVQDPHSRIC FNIGCMYTIL KNMTEAEKAF TRSINRDKHL AVAYFQRGML YYQTEKYDL AIKDLKEALI QLRGNQLIDY KILGLQFKLF ACEVLYNIAF MYAKKEEWKK AEEQLALATS MKSEPRHSKI D KAMECVWK ...String:
MSLVEAISLW NEGVLAADKK DWKGALDAFS AVQDPHSRIC FNIGCMYTIL KNMTEAEKAF TRSINRDKHL AVAYFQRGML YYQTEKYDL AIKDLKEALI QLRGNQLIDY KILGLQFKLF ACEVLYNIAF MYAKKEEWKK AEEQLALATS MKSEPRHSKI D KAMECVWK QKLYEPVVIP VGRLFRPNER QVAQLAKKDY LGKATVVASV VDQDSFSGFA PLQPQAAEPP PRPKTPEIFR AL EGEAHRV LFGFVPETKE ELQVMPGNIV FVLKKGNDNW ATVMFNGQKG LVPCNYLEPV ELRIHPQQQ

UniProtKB: UNIPROTKB: A0A024R936

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Macromolecule #5: Rac family small GTPase 1

MacromoleculeName: Rac family small GTPase 1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.463143 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG LEDYDRLRPL SYPQTDVFLI CFSLVSPAS FENVRAKWYP EVRHHCPNTP IILVGTKLDL RDDKDTIEKL KEKKLTPITY PQGLAMAKEI GAVKYLECSA L TQRGLKTV ...String:
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG LEDYDRLRPL SYPQTDVFLI CFSLVSPAS FENVRAKWYP EVRHHCPNTP IILVGTKLDL RDDKDTIEKL KEKKLTPITY PQGLAMAKEI GAVKYLECSA L TQRGLKTV FDEAIRAVLC PPPVKKRKRK CLLL

UniProtKB: Rac family small GTPase 1

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Macromolecule #6: 7D5 Fab heavy chain

MacromoleculeName: 7D5 Fab heavy chain / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 27.603949 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKKNIAFLLA SMFVFSIATN AYADVQLQES GPGLVKPSQS LSLTCSVTGY SLTSGSFWSW IRQFPGNKLE WMGYITYDGT SHFNPSLKS RFSITRDTSK NQFFLKLNSV TTEDTATYYC TRDPYRYDAM DFWGQGTSVT VSSAKTTPPS VYPLAPGSAA Q TNSMVTLG ...String:
MKKNIAFLLA SMFVFSIATN AYADVQLQES GPGLVKPSQS LSLTCSVTGY SLTSGSFWSW IRQFPGNKLE WMGYITYDGT SHFNPSLKS RFSITRDTSK NQFFLKLNSV TTEDTATYYC TRDPYRYDAM DFWGQGTSVT VSSAKTTPPS VYPLAPGSAA Q TNSMVTLG CLVKGYFPEP VTVTWNSGSL SSGVHTFPAV LQSDLYTLSS SVTVPSSTWP SETVTCNVAH PASSTKVDKK IV PRDLEHH HHHH

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Macromolecule #7: 7D5 Fab light chain

MacromoleculeName: 7D5 Fab light chain / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 26.238188 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKKNIAFLLA SMFVFSIATN AYADIQLTQT TSSLSASLGD RVTISCRASQ DISNYLNWYQ QKPDGTVKLL IYYTSKLHSG VPSRFTASG SGRDYSLAIS NLEQEDIATY FCQQVFSLPW TFGGGTKLEI KRADAAPTVS IFPPSSEQLT SGGASVVCFL N NFYPKDIN ...String:
MKKNIAFLLA SMFVFSIATN AYADIQLTQT TSSLSASLGD RVTISCRASQ DISNYLNWYQ QKPDGTVKLL IYYTSKLHSG VPSRFTASG SGRDYSLAIS NLEQEDIATY FCQQVFSLPW TFGGGTKLEI KRADAAPTVS IFPPSSEQLT SGGASVVCFL N NFYPKDIN VKWKIDGSER QNGVLNSWTD QDSKDSTYSM SSTLTLTKDE YERHNSYTCE ATHKTSTSPI VKSFNRNE

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Macromolecule #9: PROTOPORPHYRIN IX CONTAINING FE

MacromoleculeName: PROTOPORPHYRIN IX CONTAINING FE / type: ligand / ID: 9 / Number of copies: 2 / Formula: HEM
Molecular weightTheoretical: 616.487 Da
Chemical component information

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

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Macromolecule #10: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 10 / Number of copies: 2 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Macromolecule #11: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 11 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #12: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

MacromoleculeName: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
type: ligand / ID: 12 / Number of copies: 1 / Formula: NDP
Molecular weightTheoretical: 745.421 Da
Chemical component information

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

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Macromolecule #13: DIHYDROFLAVINE-ADENINE DINUCLEOTIDE

MacromoleculeName: DIHYDROFLAVINE-ADENINE DINUCLEOTIDE / type: ligand / ID: 13 / Number of copies: 1 / Formula: FDA
Molecular weightTheoretical: 787.566 Da
Chemical component information

ChemComp-FDA:
DIHYDROFLAVINE-ADENINE DINUCLEOTIDE

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Macromolecule #14: GUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 14 / Number of copies: 1 / 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 #15: water

MacromoleculeName: water / type: ligand / ID: 15 / Number of copies: 1 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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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 (6k x 4k) / Average electron dose: 52.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.79 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 209359
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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