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- PDB-7q21: III2-IV2 respiratory supercomplex from Corynebacterium glutamicum -

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Entry
Database: PDB / ID: 7q21
TitleIII2-IV2 respiratory supercomplex from Corynebacterium glutamicum
Components
  • (Co-purified unknown peptide built as polyALA ...) x 2
  • (Cytochrome bc1 complex cytochrome ...) x 2
  • (Cytochrome c oxidase subunit ...) x 3
  • (Uncharacterized ...) x 2
  • Actinobacterial supercomplex, subunit C (AscC)
  • Co-purified unknown transmembrane helices built as polyALA (AscD)
  • Cytochrome bc1 complex Rieske iron-sulfur subunit
  • Cytochrome c oxidase polypeptide 4
  • Hypothetical membrane protein
KeywordsELECTRON TRANSPORT / MEMBRANE PROTEIN / CRYO-EM / RESPIRATORY SUPERCOMPLEX / ACTINOBACTERIA
Function / homology
Function and homology information


aerobic electron transport chain / cytochrome-c oxidase / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / oxidative phosphorylation / electron transport coupled proton transport / cytochrome-c oxidase activity / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / respirasome / respiratory electron transport chain ...aerobic electron transport chain / cytochrome-c oxidase / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / oxidative phosphorylation / electron transport coupled proton transport / cytochrome-c oxidase activity / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / respirasome / respiratory electron transport chain / monooxygenase activity / 2 iron, 2 sulfur cluster binding / iron ion binding / copper ion binding / heme binding / membrane / metal ion binding / plasma membrane
Similarity search - Function
Protein of unknown function DUF2631 / Protein of unknown function (DUF2631) / QcrA subunit, N-terminal / QcrA subunit N-terminal region / Cytochrome bc1 complex, cytochrome c subunit / Cytochrome c oxidase subunit IV, actinobacteria / Cytochrome c oxidase subunit IV / Cytochrome b(N-terminal)/b6/petB / Cytochrome c oxidase, subunit I bacterial type / Cytochrome C oxidase, cbb3-type, subunit III ...Protein of unknown function DUF2631 / Protein of unknown function (DUF2631) / QcrA subunit, N-terminal / QcrA subunit N-terminal region / Cytochrome bc1 complex, cytochrome c subunit / Cytochrome c oxidase subunit IV, actinobacteria / Cytochrome c oxidase subunit IV / Cytochrome b(N-terminal)/b6/petB / Cytochrome c oxidase, subunit I bacterial type / Cytochrome C oxidase, cbb3-type, subunit III / Cytochrome c oxidase subunit III / Cytochrome c oxidase subunit III-like / Cytochrome c oxidase, subunit III, 4-helical bundle / Cytochrome c oxidase subunit III / Heme-copper oxidase subunit III family profile. / Cytochrome c oxidase subunit III-like superfamily / Cytochrome C oxidase subunit II, transmembrane domain / Cytochrome oxidase subunit II transmembrane region profile. / Cytochrome c/quinol oxidase subunit II / Copper centre Cu(A) / CO II and nitrous oxide reductase dinuclear copper centers signature. / Cytochrome C oxidase subunit II, transmembrane domain superfamily / Cytochrome c oxidase, subunit I, copper-binding site / Heme-copper oxidase catalytic subunit, copper B binding region signature. / Cytochrome c oxidase-like, subunit I domain / Cytochrome oxidase subunit I profile. / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Cytochrome c oxidase subunit I / Cytochrome c oxidase-like, subunit I superfamily / Cytochrome C and Quinol oxidase polypeptide I / Di-haem cytochrome, transmembrane / Cytochrome C oxidase subunit II, periplasmic domain / Rieske iron-sulphur protein / Cytochrome c oxidase subunit II-like C-terminal / Cytochrome oxidase subunit II copper A binding domain profile. / Cytochrome c / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Cupredoxin
Similarity search - Domain/homology
Chem-7PH / Chem-9XX / Chem-9YF / CARDIOLIPIN / COPPER (II) ION / FE2/S2 (INORGANIC) CLUSTER / HEME-AS / HEME C / PROTOPORPHYRIN IX CONTAINING FE / MENAQUINONE-9 ...Chem-7PH / Chem-9XX / Chem-9YF / CARDIOLIPIN / COPPER (II) ION / FE2/S2 (INORGANIC) CLUSTER / HEME-AS / HEME C / PROTOPORPHYRIN IX CONTAINING FE / MENAQUINONE-9 / PALMITIC ACID / TRIDECANE / DOCOSANE / Cytochrome c oxidase subunit 1 / Cytochrome bc1 complex Rieske iron-sulfur subunit / Cytochrome bc1 complex cytochrome b subunit / Uncharacterized protein Cgl2664/cg2949 / Cytochrome c oxidase subunit 2 / Cytochrome c oxidase polypeptide 4 / Cytochrome bc1 complex cytochrome c subunit / Uncharacterized membrane protein Cgl2017/cg2211 / Uncharacterized protein / Hypothetical membrane protein / Cytochrome c oxidase subunit 3
Similarity search - Component
Biological speciesCorynebacterium glutamicum ATCC 13032 (bacteria)
Corynebacterium glutamicum (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsKovalova, T. / Moe, A. / Krol, S. / Yanofsky, D.J. / Bott, M. / Sjostrand, D. / Rubinstein, J.L. / Hogbom, M. / Brzezinski, P.
Funding support Canada, 4items
OrganizationGrant numberCountry
Knut and Alice Wallenberg Foundation Canada
Swedish Research Council Canada
Canadian Institutes of Health Research (CIHR)PJT162186 Canada
Canada Research Chairs Canada
CitationJournal: Structure / Year: 2022
Title: The respiratory supercomplex from C. glutamicum.
Authors: Agnes Moe / Terezia Kovalova / Sylwia Król / David J Yanofsky / Michael Bott / Dan Sjöstrand / John L Rubinstein / Martin Högbom / Peter Brzezinski /
Abstract: Corynebacterium glutamicum is a preferentially aerobic gram-positive bacterium belonging to the phylum Actinobacteria, which also includes the pathogen Mycobacterium tuberculosis. In these bacteria, ...Corynebacterium glutamicum is a preferentially aerobic gram-positive bacterium belonging to the phylum Actinobacteria, which also includes the pathogen Mycobacterium tuberculosis. In these bacteria, respiratory complexes III and IV form a CIIICIV supercomplex that catalyzes oxidation of menaquinol and reduction of dioxygen to water. We isolated the C. glutamicum supercomplex and used cryo-EM to determine its structure at 2.9 Å resolution. The structure shows a central CIII dimer flanked by a CIV on two sides. A menaquinone is bound in each of the Q and Q sites in each CIII and an additional menaquinone is positioned ∼14 Å from heme b. A di-heme cyt. cc subunit electronically connects each CIII with an adjacent CIV, with the Rieske iron-sulfur protein positioned with the iron near heme b. Multiple subunits interact to form a convoluted sub-structure at the cytoplasmic side of the supercomplex, which defines a path for proton transfer into CIV.
History
DepositionOct 22, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 2, 2022Provider: repository / Type: Initial release
Revision 1.1Mar 16, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.year

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Structure visualization

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Assembly

Deposited unit
Y: Co-purified unknown transmembrane helices built as polyALA (AscD)
E: Cytochrome c oxidase subunit 3
H: Uncharacterized membrane protein Cgl2017/cg2211
F: Cytochrome c oxidase polypeptide 4
G: Cytochrome c oxidase subunit 2
D: Cytochrome c oxidase subunit 1
A: Cytochrome bc1 complex Rieske iron-sulfur subunit
L: Uncharacterized protein Cgl2664/cg2949
B: Cytochrome bc1 complex cytochrome b subunit
C: Cytochrome bc1 complex cytochrome c subunit
y: Co-purified unknown transmembrane helices built as polyALA (AscD)
e: Cytochrome c oxidase subunit 3
h: Uncharacterized membrane protein Cgl2017/cg2211
f: Cytochrome c oxidase polypeptide 4
g: Cytochrome c oxidase subunit 2
d: Cytochrome c oxidase subunit 1
a: Cytochrome bc1 complex Rieske iron-sulfur subunit
l: Uncharacterized protein Cgl2664/cg2949
b: Cytochrome bc1 complex cytochrome b subunit
c: Cytochrome bc1 complex cytochrome c subunit
X: Co-purified unknown peptide built as polyALA (AscE)
x: Co-purified unknown peptide built as polyALA (AscE)
V: Actinobacterial supercomplex, subunit C (AscC)
v: Actinobacterial supercomplex, subunit C (AscC)
K: Hypothetical membrane protein
k: Hypothetical membrane protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)735,452118
Polymers680,96526
Non-polymers54,48792
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: mass spectrometry, gel filtration, mass spectrometry, native gel electrophoresis, microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 5 types, 10 molecules YyFfAaVvKk

#1: Protein Co-purified unknown transmembrane helices built as polyALA (AscD)


Mass: 8188.084 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum ATCC 13032 (bacteria)
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
#4: Protein Cytochrome c oxidase polypeptide 4 / Cytochrome aa3 subunit 4 / Cytochrome c oxidase polypeptide IV


Mass: 15557.285 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (bacteria)
Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025
Gene: ctaF, Cgl2194, cg2408
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q8NNK3, cytochrome-c oxidase
#7: Protein Cytochrome bc1 complex Rieske iron-sulfur subunit / Cytochrome bc1 reductase complex subunit QcrA / Menaquinol--cytochrome c reductase iron-sulfur ...Cytochrome bc1 reductase complex subunit QcrA / Menaquinol--cytochrome c reductase iron-sulfur subunit / Rieske iron-sulfur protein


Mass: 45232.207 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (bacteria)
Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025
Gene: qcrA, Cgl2190, cg2404
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q79VE8
#13: Protein Actinobacterial supercomplex, subunit C (AscC)


Mass: 8373.271 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (bacteria)
Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025
Gene: Cgl0818
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q8NS61
#14: Protein Hypothetical membrane protein


Mass: 6628.905 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (bacteria)
Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025
Gene: Cgl0673
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q8NSJ8

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Cytochrome c oxidase subunit ... , 3 types, 6 molecules EeGgDd

#2: Protein Cytochrome c oxidase subunit 3 / / Cytochrome aa3 subunit 3 / Cytochrome c oxidase polypeptide III


Mass: 22457.217 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (bacteria)
Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025
Gene: ctaE, Cgl2192, cg2406
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q9AEL8, cytochrome-c oxidase
#5: Protein Cytochrome c oxidase subunit 2 / / Cytochrome aa3 subunit 2 / Cytochrome c oxidase polypeptide II / Oxidase aa(3) subunit 2


Mass: 39665.562 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (bacteria)
Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025
Gene: ctaC, Cgl2195, cg2409
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q8NNK2, cytochrome-c oxidase
#6: Protein Cytochrome c oxidase subunit 1 / / Cytochrome aa3 subunit 1 / Cytochrome c oxidase polypeptide I


Mass: 66340.164 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (bacteria)
Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025
Gene: ctaD, Cgl2523, cg2780
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q79VD7, cytochrome-c oxidase

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Uncharacterized ... , 2 types, 4 molecules HhLl

#3: Protein Uncharacterized membrane protein Cgl2017/cg2211 / P20


Mass: 16385.588 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum ATCC 13032 (bacteria)
Gene: Cgl2017, cg2211
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q8NP09
#8: Protein Uncharacterized protein Cgl2664/cg2949 / P29


Mass: 20025.750 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (bacteria)
Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025
Gene: Cgl2664, cg2949
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q8NMB4

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Cytochrome bc1 complex cytochrome ... , 2 types, 4 molecules BbCc

#9: Protein Cytochrome bc1 complex cytochrome b subunit / Cytochrome bc1 reductase complex subunit QcrB / Menaquinol--cytochrome c reductase cytochrome b subunit


Mass: 59863.699 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum ATCC 13032 (bacteria)
Gene: qcrB, Cgl2189, cg2403
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q79VE9, quinol-cytochrome-c reductase
#10: Protein Cytochrome bc1 complex cytochrome c subunit / Cytochrome c1 / Cytochrome bc1 reductase complex subunit Qcrc / Menaquinol--cytochrome c reductase ...Cytochrome c1 / Cytochrome bc1 reductase complex subunit Qcrc / Menaquinol--cytochrome c reductase cytochrome c subunit


Mass: 29898.850 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (bacteria)
Strain: ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025
Gene: qcrC, Cgl2191, cg2405
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
References: UniProt: Q8NNK5, quinol-cytochrome-c reductase

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Co-purified unknown peptide built as polyALA ... , 2 types, 2 molecules Xx

#11: Protein/peptide Co-purified unknown peptide built as polyALA (AscE)


Mass: 1823.254 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum ATCC 13032 (bacteria)
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)
#12: Protein/peptide Co-purified unknown peptide built as polyALA (AscE)


Mass: 1908.359 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Corynebacterium glutamicum ATCC 13032 (bacteria)
Production host: Corynebacterium glutamicum ATCC 13032 (bacteria)

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Non-polymers , 15 types, 92 molecules

#15: Chemical
ChemComp-CDL / CARDIOLIPIN / DIPHOSPHATIDYL GLYCEROL / BIS-(1,2-DIACYL-SN-GLYCERO-3-PHOSPHO)-1',3'-SN-GLYCEROL / Cardiolipin


Mass: 1464.043 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C81H156O17P2 / Comment: phospholipid*YM
#16: Chemical
ChemComp-7PH / (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate / PHOSPHATIDIC ACID / Phosphatidic acid


Mass: 564.732 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C29H57O8P
#17: Chemical
ChemComp-TRD / TRIDECANE / LIPID FRAGMENT / Tridecane


Mass: 184.361 Da / Num. of mol.: 18 / Source method: obtained synthetically / Formula: C13H28
#18: Chemical
ChemComp-9XX / (2S)-1-(hexadecanoyloxy)propan-2-yl (10S)-10-methyloctadecanoate / (S)-1-(palmitoyloxy)propan-2-yl (S)-10-methyloctadecanoate


Mass: 594.992 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C38H74O4
#19: Chemical ChemComp-TWT / DOCOSANE / Higher alkanes


Mass: 310.601 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C22H46
#20: Chemical
ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Cu
#21: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#22: Chemical
ChemComp-HAS / HEME-AS


Mass: 920.954 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C54H64FeN4O6
#23: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#24: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe2S2
#25: Chemical
ChemComp-MQ9 / MENAQUINONE-9 / Vitamin K2


Mass: 785.233 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C56H80O2 / Feature type: SUBJECT OF INVESTIGATION
#26: Chemical
ChemComp-9YF / (2R)-2-(hexadecanoyloxy)-3-{[(S)-hydroxy{[(1R,2R,3R,4R,5R,6S)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}propyl (9S)-9-methyloctadecanoate


Mass: 853.112 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C44H85O13P
#27: Chemical
ChemComp-PLM / PALMITIC ACID / Palmitic acid


Mass: 256.424 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C16H32O2
#28: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#29: Chemical
ChemComp-HEC / HEME C / Heme C


Mass: 618.503 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H34FeN4O4

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Details

Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: The respiratory supercomplex / Type: COMPLEX / Entity ID: #1-#14 / Source: RECOMBINANT
Molecular weightUnits: KILODALTONS/NANOMETER / Experimental value: YES
Source (natural)Organism: Corynebacterium glutamicum ATCC 13032 (bacteria)
Source (recombinant)Organism: Corynebacterium glutamicum ATCC 13032 (bacteria)
Buffer solutionpH: 7.5
SpecimenConc.: 10 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: C-flat-2/2
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 276 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / C2 aperture diameter: 70 µm
Image recordingAverage exposure time: 8 sec. / Electron dose: 55 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

SoftwareName: REFMAC / Version: 5.8.0257 / Classification: refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 65391 / Symmetry type: POINT
RefinementResolution: 3→328.6 Å / Cor.coef. Fo:Fc: 0.799
RfactorNum. reflection% reflection
Rwork0.37382 --
obs0.37382 2752401 100 %
Displacement parametersBiso mean: 56.633 Å2
Baniso -1Baniso -2Baniso -3
1--0.34 Å20.8 Å20.03 Å2
2---0.67 Å2-0.01 Å2
3---1.01 Å2
LS refinement shellHighest resolution: 3 Å /
Rfactor% reflection
Rfree0 -
Rwork1.878 -
obs-100 %

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