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- EMDB-24612: CLC-ec1 at pH 4.5 100mM Cl Turn -

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Basic information

Entry
Database: EMDB / ID: EMD-24612
TitleCLC-ec1 at pH 4.5 100mM Cl Turn
Map dataCLC-ec1 100 mM Cl pH 4.5 TURN
Sample
  • Complex: Structure of ecCLC at pH 4.5 in 100mM Cl
    • Protein or peptide: H(+)/Cl(-) exchange transporter ClcA
Function / homologyChloride channel, ClcA / Chloride channel, voltage gated / Chloride channel, core / Voltage gated chloride channel / voltage-gated chloride channel activity / antiporter activity / plasma membrane / H(+)/Cl(-) exchange transporter ClcA
Function and homology information
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.72 Å
AuthorsFortea E / Boudker O / Accardi A
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: To Be Published
Title: Structural basis of common gate activation in CLC transporters
Authors: Fortea E / Lee S / Argyros Y / Chadda R / Ciftci D / Huysmans G / Robertson JL / Boudker O / Accardi A
History
DepositionAug 3, 2021-
Header (metadata) releaseNov 16, 2022-
Map releaseNov 16, 2022-
UpdateNov 16, 2022-
Current statusNov 16, 2022Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_24612.png

Downloads & links

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Map

FileDownload / File: emd_24612.map.gz / Format: CCP4 / Size: 28.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCLC-ec1 100 mM Cl pH 4.5 TURN
Voxel sizeX=Y=Z: 1.048 Å
Density
Contour LevelBy AUTHOR: 0.174
Minimum - Maximum-0.7517255 - 1.0962663
Average (Standard dev.)0.0045061614 (±0.033945117)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions196196196
Spacing196196196
CellA=B=C: 205.40799 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Structure of ecCLC at pH 4.5 in 100mM Cl

EntireName: Structure of ecCLC at pH 4.5 in 100mM Cl
Components
  • Complex: Structure of ecCLC at pH 4.5 in 100mM Cl
    • Protein or peptide: H(+)/Cl(-) exchange transporter ClcA

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Supramolecule #1: Structure of ecCLC at pH 4.5 in 100mM Cl

SupramoleculeName: Structure of ecCLC at pH 4.5 in 100mM Cl / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli (E. coli)
Recombinant expressionOrganism: Escherichia coli (E. coli)
Molecular weightExperimental: 100 kDa/nm

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Macromolecule #1: H(+)/Cl(-) exchange transporter ClcA

MacromoleculeName: H(+)/Cl(-) exchange transporter ClcA / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 50.390402 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKTDTPSLET PQAARLRRRQ LIRQLLERDK TPLAILFMAA VVGTLVGLAA VAFDKGVAWL QNQRMGALVH TADNYPLLLT VAFLCSAVL AMFGYFLVRK YAPEAGGSGI PEIEGALEDQ RPVRWWRVLP VKFFGGLGTL GGGMVLGREG PTVQIGGNIG R MVLDIFRL ...String:
MKTDTPSLET PQAARLRRRQ LIRQLLERDK TPLAILFMAA VVGTLVGLAA VAFDKGVAWL QNQRMGALVH TADNYPLLLT VAFLCSAVL AMFGYFLVRK YAPEAGGSGI PEIEGALEDQ RPVRWWRVLP VKFFGGLGTL GGGMVLGREG PTVQIGGNIG R MVLDIFRL KGDEARHTLL ATGAAAGLAA AFNAPLAGIL FIIEEMRPQF RYTLISIKAV FIGVIMSTIM YRIFNHEVAL ID VGKLSDA PLNTLWLYLI LGIIFGIFGP IFNKWVLGMQ DLLHRVHGGN ITKWVLMGGA IGGLCGLLGF VAPATSGGGF NLI PIATAG NFSMGMLVFI FVARVITTLL CFSSGAPGGI FAPMLALGTV LGTAFGMVAV ELFPQYHLEA GTFAIAGMGA LLAA SIRAP LTGIILVLEM TDNYQLILPM IITGLGATLL AQFTGGKPLY SAILARTLAK QEAEQLARSK AASASENT

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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

Concentration1.7 mg/mL
BufferpH: 4.5
GridModel: UltrAuFoil R1.2/1.3
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 294.15 K

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 72.61 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.72 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 59069

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