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- EMDB-39568: Cryo-EM structure of the dystrophin glycoprotein complex -

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Basic information

Entry
Database: EMDB / ID: EMD-39568
TitleCryo-EM structure of the dystrophin glycoprotein complex
Map data
Sample
  • Complex: dystrophin glycoprotein complex, DGC
    • Protein or peptide: x 9 types
  • Ligand: x 5 types
Keywordscomplex membrane stability signaling / STRUCTURAL PROTEIN
Function / homology
Function and homology information


dystrobrevin complex / olfactory nerve structural organization / sarcoglycan complex / O-linked glycosylation / establishment of blood-nerve barrier / striated muscle cell development / establishment of glial blood-brain barrier / dystroglycan complex / nerve maturation / connective tissue development ...dystrobrevin complex / olfactory nerve structural organization / sarcoglycan complex / O-linked glycosylation / establishment of blood-nerve barrier / striated muscle cell development / establishment of glial blood-brain barrier / dystroglycan complex / nerve maturation / connective tissue development / retrograde trans-synaptic signaling by trans-synaptic protein complex / walking behavior / positive regulation of basement membrane assembly involved in embryonic body morphogenesis / regulation of cellular response to growth factor stimulus / Regulation of expression of SLITs and ROBOs / regulation of skeletal muscle contraction / negative regulation of peptidyl-cysteine S-nitrosylation / contractile ring / regulation of voltage-gated calcium channel activity / regulation of gastrulation / cardiac muscle cell action potential / calcium-dependent cell-matrix adhesion / reactive oxygen species biosynthetic process / morphogenesis of an epithelial sheet / glucose import in response to insulin stimulus / nucleus localization / coronary vasculature morphogenesis / dystrophin-associated glycoprotein complex / positive regulation of sodium ion transmembrane transporter activity / microtubule anchoring / vascular associated smooth muscle cell development / laminin-1 binding / response to denervation involved in regulation of muscle adaptation / postsynaptic specialization / matrix side of mitochondrial inner membrane / Formation of the dystrophin-glycoprotein complex (DGC) / neurofilament / cell-substrate junction / myotube cell development / Striated Muscle Contraction / positive regulation of myelination / basement membrane organization / photoreceptor ribbon synapse / dystroglycan binding / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / heart process / lamin binding / cellular response to cholesterol / vinculin binding / regulation of epithelial to mesenchymal transition / myelination in peripheral nervous system / branching involved in salivary gland morphogenesis / skeletal muscle tissue regeneration / costamere / astrocyte projection / commissural neuron axon guidance / membrane organization / protein-containing complex localization / muscle cell development / neuron projection terminus / negative regulation of peptidyl-serine phosphorylation / node of Ranvier / cardiac muscle cell contraction / angiogenesis involved in wound healing / limb development / synaptic transmission, cholinergic / cardiac muscle cell development / axon regeneration / structural constituent of muscle / positive regulation of cell-matrix adhesion / muscle cell cellular homeostasis / nitric-oxide synthase binding / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / muscle organ development / response to muscle activity / epithelial tube branching involved in lung morphogenesis / regulation of synapse organization / alpha-actinin binding / : / membrane protein ectodomain proteolysis / basement membrane / positive regulation of oligodendrocyte differentiation / postsynaptic cytosol / regulation of ryanodine-sensitive calcium-release channel activity / plasma membrane raft / negative regulation of neuron differentiation / negative regulation of MAPK cascade / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / Schwann cell development / striated muscle contraction / response to glucose / heart morphogenesis / calcium ion homeostasis / skeletal muscle tissue development / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / cardiac muscle contraction / laminin binding / response to muscle stretch / positive regulation of neuron differentiation / tubulin binding
Similarity search - Function
Distrobrevin / Sarcoglycan complex subunit protein / Sarcoglycan alpha/epsilon / Beta-sarcoglycan / Sarcospan / Sarcoglycan gamma/delta/zeta / : / : / Sarcoglycan complex subunit protein / Sarcoglycan alpha/epsilon N-terminal domain ...Distrobrevin / Sarcoglycan complex subunit protein / Sarcoglycan alpha/epsilon / Beta-sarcoglycan / Sarcospan / Sarcoglycan gamma/delta/zeta / : / : / Sarcoglycan complex subunit protein / Sarcoglycan alpha/epsilon N-terminal domain / Sarcoglycan alpha/epsilon second domain / Dystroglycan-type cadherin-like / Dystroglycan, C-terminal / Alpha-dystroglycan domain 2 / DG-type SEA domain / Alpha-dystroglycan N-terminal domain 2 / Dystroglycan (Dystrophin-associated glycoprotein 1) / Alpha-Dystroglycan N-terminal domain 2 / DG-type SEA domain profile. / Dystroglycan-type cadherin-like domains. / Putative Ig domain / Dystrophin/utrophin / EF-hand domain, type 1 / EF-hand domain, type 2 / EF hand / EF-hand / CD20-like family / CD20-like family / : / Spectrin repeat / Spectrin repeat / Spectrin/alpha-actinin / Spectrin repeats / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Cadherin-like superfamily / Calponin homology domain / Zinc finger ZZ-type signature. / Calponin homology (CH) domain / Zinc-binding domain, present in Dystrophin, CREB-binding protein. / Zinc finger, ZZ type / Zinc finger, ZZ-type / Zinc finger, ZZ-type superfamily / Zinc finger ZZ-type profile. / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / WW domain / WW/rsp5/WWP domain signature. / WW domain superfamily / WW/rsp5/WWP domain profile. / Domain with 2 conserved Trp (W) residues / WW domain / EF-hand domain pair / Immunoglobulin-like fold
Similarity search - Domain/homology
Dystrophin / Delta-sarcoglycan / Gamma-sarcoglycan / Beta-sarcoglycan / Alpha-sarcoglycan / Sarcospan / Dystroglycan 1 / Dystrobrevin alpha
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / Resolution: 3.5 Å
AuthorsWu JP / Yan Z / Wan L
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32271261 China
CitationJournal: Nature / Year: 2025
Title: Structure and assembly of the dystrophin glycoprotein complex.
Authors: Li Wan / Xiaofei Ge / Qikui Xu / Gaoxingyu Huang / Tiandi Yang / Kevin P Campbell / Zhen Yan / Jianping Wu /
Abstract: The dystrophin glycoprotein complex (DGC) has a crucial role in maintaining cell membrane stability and integrity by connecting the intracellular cytoskeleton with the surrounding extracellular ...The dystrophin glycoprotein complex (DGC) has a crucial role in maintaining cell membrane stability and integrity by connecting the intracellular cytoskeleton with the surrounding extracellular matrix. Dysfunction of dystrophin and its associated proteins results in muscular dystrophy, a disorder characterized by progressive muscle weakness and degeneration. Despite the important roles of the DGC in physiology and pathology, its structural details remain largely unknown, hindering a comprehensive understanding of its assembly and function. Here we isolated the native DGC from mouse skeletal muscle and obtained its high-resolution structure. Our findings unveil a markedly divergent structure from the previous model of DGC assembly. Specifically, on the extracellular side, β-, γ- and δ-sarcoglycans co-fold to form a specialized, extracellular tower-like structure, which has a central role in complex assembly by providing binding sites for α-sarcoglycan and dystroglycan. In the transmembrane region, sarcoglycans and sarcospan flank and stabilize the single transmembrane helix of dystroglycan, rather than forming a subcomplex as previously proposed. On the intracellular side, sarcoglycans and dystroglycan engage in assembly with the dystrophin-dystrobrevin subcomplex through extensive interaction with the ZZ domain of dystrophin. Collectively, these findings enhance our understanding of the structural linkage across the cell membrane and provide a foundation for the molecular interpretation of many muscular dystrophy-related mutations.
History
DepositionMar 25, 2024-
Header (metadata) releaseDec 11, 2024-
Map releaseDec 11, 2024-
UpdateFeb 12, 2025-
Current statusFeb 12, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_39568.png

Downloads & links

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Map

FileDownload / File: emd_39568.map.gz / Format: CCP4 / Size: 307.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 432 pix.
= 469.584 Å		1.09 Å/pix.
x 432 pix.
= 469.584 Å		1.09 Å/pix.
x 432 pix.
= 469.584 Å

Surface

Projections

Slices (1/3)

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.087 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.28
Minimum - Maximum-1.9093491 - 3.340943
Average (Standard dev.)-0.0012319844 (±0.043488972)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions432432432
Spacing432432432
CellA=B=C: 469.584 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_39568_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_39568_half_map_2.map
Projections & Slices
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Sample components

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Entire : dystrophin glycoprotein complex, DGC

EntireName: dystrophin glycoprotein complex, DGC
Components
  • Complex: dystrophin glycoprotein complex, DGC
    • Protein or peptide: Alpha-sarcoglycan
    • Protein or peptide: Beta-sarcoglycan
    • Protein or peptide: Dystrobrevin alpha
    • Protein or peptide: Delta-sarcoglycan
    • Protein or peptide: Dystrophin
    • Protein or peptide: Gamma-sarcoglycan
    • Protein or peptide: unknown segment
    • Protein or peptide: Beta-dystroglycan
    • Protein or peptide: Sarcospan
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: CHOLESTEROL
  • Ligand: ZINC ION
  • Ligand: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
  • Ligand: CALCIUM ION

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Supramolecule #1: dystrophin glycoprotein complex, DGC

SupramoleculeName: dystrophin glycoprotein complex, DGC / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Mus musculus (house mouse)

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Macromolecule #1: Alpha-sarcoglycan

MacromoleculeName: Alpha-sarcoglycan / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 32.539186 KDa
SequenceString: QQTTLHLLVG RVFVHPLEHA TFLRLPEHVA VPPTVRLTYH AHLQGHPDLP RWLHYTQRSP YNPGFLYGSP TPEDRGYQVI EVTAYNRDS FDTTRQRLLL LIGDPEGPRL PYQAEFLVRS HDVEEVLPTT PANRFLTALG GLWEPGELQL LNITSALDRG G RVPLPIEG ...String:
QQTTLHLLVG RVFVHPLEHA TFLRLPEHVA VPPTVRLTYH AHLQGHPDLP RWLHYTQRSP YNPGFLYGSP TPEDRGYQVI EVTAYNRDS FDTTRQRLLL LIGDPEGPRL PYQAEFLVRS HDVEEVLPTT PANRFLTALG GLWEPGELQL LNITSALDRG G RVPLPIEG RKEGVYIKVG SATPFSTCLK MVASPDSYAR CAQGQPPLLS CYDTLAPHFR VDWCNVSLVD KSVPEPLDEV PT PGDGILE HDPFFCPPTE ATDRDFLTDA LVTLLVPLLV ALLLTLLLAY IMCF

UniProtKB: Alpha-sarcoglycan

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Macromolecule #2: Beta-sarcoglycan

MacromoleculeName: Beta-sarcoglycan / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 28.729967 KDa
SequenceString: HKTGLRGRKG NLAICVIVLL FILAVINLLI TLVIWAVIRI GPNGCDSMEF HESGLLRFKQ VSDMGVIHPL YKSTVGGRRN ENLVITGNN QPIVFQQGTT KLSVEKNKTS ITSDIGMQFF DPRTHNILFS TDYETHEFHL PSGVKSLNVQ KASTERITSN A TSDLNIKV ...String:
HKTGLRGRKG NLAICVIVLL FILAVINLLI TLVIWAVIRI GPNGCDSMEF HESGLLRFKQ VSDMGVIHPL YKSTVGGRRN ENLVITGNN QPIVFQQGTT KLSVEKNKTS ITSDIGMQFF DPRTHNILFS TDYETHEFHL PSGVKSLNVQ KASTERITSN A TSDLNIKV DGRAIVRGNE GVFIMGKTIE FHMGGDVELK AENSIILNGT VMVSPTRLPS SSSGDQSGSG DWVRYKLCMC AD GTLFKVQ VTGHNMGCQV SDNPCG

UniProtKB: Beta-sarcoglycan

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Macromolecule #3: Dystrobrevin alpha

MacromoleculeName: Dystrobrevin alpha / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 23.363234 KDa
SequenceString: LSTYRTACKL RFVQKKCNLH LVDIWNVIEA LRENALNNLD PNIELNVARL EAVLSTIFYQ LNKRMPTTHQ IHVEQSISLL LNFLLAAFD PEGHGKISVF AVKMALATLC GGKIMDKLRY IFSMISDSSG VMVYGRYDQF LREVLKLPTA VFEGPSFGYT E QSARSCFS ...String:
LSTYRTACKL RFVQKKCNLH LVDIWNVIEA LRENALNNLD PNIELNVARL EAVLSTIFYQ LNKRMPTTHQ IHVEQSISLL LNFLLAAFD PEGHGKISVF AVKMALATLC GGKIMDKLRY IFSMISDSSG VMVYGRYDQF LREVLKLPTA VFEGPSFGYT E QSARSCFS QQKKVTLNGF LDTLMSDPPP QCLVWLPLLH RLANVENV

UniProtKB: Dystrobrevin alpha

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Macromolecule #4: Delta-sarcoglycan

MacromoleculeName: Delta-sarcoglycan / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 29.1911 KDa
SequenceString: YGWRKRCLYF FVLLLMILIL VNLAMTIWIL KVMNFTIDGM GNLRITEKGL KLEGDSEFLQ PLYAKEIKSR PGNALYFKSA RNVTVNILN DQTKVLTQLV TGPKAVEAYG KRFEVKTVSG KLLFSADDSE VVVGAERLRV LGAEGTVFPK SIETPNVRAD P FKELRLES ...String:
YGWRKRCLYF FVLLLMILIL VNLAMTIWIL KVMNFTIDGM GNLRITEKGL KLEGDSEFLQ PLYAKEIKSR PGNALYFKSA RNVTVNILN DQTKVLTQLV TGPKAVEAYG KRFEVKTVSG KLLFSADDSE VVVGAERLRV LGAEGTVFPK SIETPNVRAD P FKELRLES PTRSLVMEAP KGVEINAEAG NMEAICRSEL RLESKDGEIK LDAAKIKLPR LPRGSYTPTG TRQKVFEVCV CA NGRLFLS QAGTGSTCQI NTSVCL

UniProtKB: Delta-sarcoglycan

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Macromolecule #5: Dystrophin

MacromoleculeName: Dystrophin / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 38.371391 KDa
SequenceString: YYINHETQTT CWDHPKMTEL YQSLADLNNV RFSAYRTAMK LRRLQKALCL DLLSLSAACD ALDQHNLKQN DQPMDILQII NCLTTIYDR LEQEHNNLVN VPLCVDMCLN WLLNVYDTGR TGRIRVLSFK TGIISLCKAH LEDKYRYLFK QVASSTGFCD Q RRLGLLLH ...String:
YYINHETQTT CWDHPKMTEL YQSLADLNNV RFSAYRTAMK LRRLQKALCL DLLSLSAACD ALDQHNLKQN DQPMDILQII NCLTTIYDR LEQEHNNLVN VPLCVDMCLN WLLNVYDTGR TGRIRVLSFK TGIISLCKAH LEDKYRYLFK QVASSTGFCD Q RRLGLLLH DSIQIPRQLG EVASFGGSNI EPSVRSCFQF ANNKPEIEAA LFLDWMRLEP QSMVWLPVLH RVAAAETAKH QA KCNICKE CPIIGFRYRS LKHFNYDICQ SCFFSGRVAK GHKMHYPMVE YCTPTTSGED VRDFAKVLKN KFRTKRYFAK HPR MGYLPV QTVLE

UniProtKB: Dystrophin

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Macromolecule #6: Gamma-sarcoglycan

MacromoleculeName: Gamma-sarcoglycan / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 28.956158 KDa
SequenceString: GIYGWRKRCL YLFVLLLLAI LVVNLALTIW ILKVMWFSPI GMGHLHVTAD GLRLEGESEF LFPLYAKEIR SRVDSSLLLQ STQNVTVSA RNSEGEVTGR VKVGAQMVEV QSQHFQINSE DGKPLFSAEE QDVVVGTGRL RVTGPEGALF EHSVETPLVR A DPFQDLRL ...String:
GIYGWRKRCL YLFVLLLLAI LVVNLALTIW ILKVMWFSPI GMGHLHVTAD GLRLEGESEF LFPLYAKEIR SRVDSSLLLQ STQNVTVSA RNSEGEVTGR VKVGAQMVEV QSQHFQINSE DGKPLFSAEE QDVVVGTGRL RVTGPEGALF EHSVETPLVR A DPFQDLRL ESPTRSLSMD APRGVHVKAN AGKLEALSQM DIILQSSEGV LVLDAETVGL TKLKQGTQGP AGSSNGFYEI CA CPDGKLY LSMAGEVTTC EEHSHVCL

UniProtKB: Gamma-sarcoglycan

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Macromolecule #7: unknown segment

MacromoleculeName: unknown segment / type: protein_or_peptide / ID: 7 / Details: unassigned / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 559.741 Da
SequenceString:
ALPKM

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Macromolecule #8: Beta-dystroglycan

MacromoleculeName: Beta-dystroglycan / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 31.934459 KDa
SequenceString: NQRPELKNHI DRVDAWVGTY FEVKIPSDTF YDNEDTTTDK LKLTLKLREQ QLVGEKSWVQ FNSNSQLMYG LPDSSHVGKH EYFMHATDK GGLSAVDAFE IHVHKRPQGD KAPARFKARL AGDPAPVVND IHKKIALVKK LAFAFGDRNC SSITLQNITR G SIVVEWTN ...String:
NQRPELKNHI DRVDAWVGTY FEVKIPSDTF YDNEDTTTDK LKLTLKLREQ QLVGEKSWVQ FNSNSQLMYG LPDSSHVGKH EYFMHATDK GGLSAVDAFE IHVHKRPQGD KAPARFKARL AGDPAPVVND IHKKIALVKK LAFAFGDRNC SSITLQNITR G SIVVEWTN NTLPLEPCPK EQIIGLSRRI ADENGKPRPA FSNALEPDFK ALSIAVTGSG SCRHLQFIPV APPSPGSSAA PA TEVPDRD PEKSSEDDVY LHTVIPAVVV AAILLIAGII AMICYRKKRK GK

UniProtKB: Dystroglycan 1

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Macromolecule #9: Sarcospan

MacromoleculeName: Sarcospan / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 19.917953 KDa
SequenceString:
CRFPLLLALL QLALGIAVTV LGFLMASISP SLLVRDTPFW AGSIVCVVAY LGLFMLCVSY QVDERTCVQF SMKVFYFLLS ALGLMVCML AVAFAAHHYS LLAQFTCETS LDSCQCKLPS SEPLSRAFVY RDVTDCTSVT GTFKLFLIIQ MVLNLVCGLV C LLACFVMW KHRYQVFYVG V

UniProtKB: Sarcospan

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Macromolecule #14: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 14 / Number of copies: 3 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

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

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Macromolecule #15: CHOLESTEROL

MacromoleculeName: CHOLESTEROL / type: ligand / ID: 15 / Number of copies: 3 / Formula: CLR
Molecular weightTheoretical: 386.654 Da
Chemical component information

ChemComp-CLR:
CHOLESTEROL

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Macromolecule #16: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 16 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #17: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phospho...

MacromoleculeName: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine
type: ligand / ID: 17 / Number of copies: 1 / Formula: P5S
Molecular weightTheoretical: 792.075 Da
Chemical component information

ChemComp-P5S:
O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine

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Macromolecule #18: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 18 / Number of copies: 1 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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Experimental details

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Structure determination

Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4 / Details: 25 mM MOPS-Na, 150 mM NaCl, 2 mM CaCl2, 0.01% GDN

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k 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: 1.9000000000000001 µm / Nominal defocus min: 1.4000000000000001 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 499658
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementProtocol: FLEXIBLE FIT
Output model

PDB-8yt8:
Cryo-EM structure of the dystrophin glycoprotein complex

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