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- EMDB-71746: CsgG nanopore in complex with designed CsgX1C -

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Basic information

Entry
Database: EMDB / ID: EMD-71746
TitleCsgG nanopore in complex with designed CsgX1C
Map data
Sample
  • Complex: Nanopore assembly of CsgG nonamer with CsgX1C nonamer
    • Protein or peptide: CsgX1C
    • Protein or peptide: Curli production assembly/transport component CsgG
Keywordscomplex / de novo design / nanopore / MEMBRANE PROTEIN
Function / homologyCurli production assembly/transport component CsgG / Curli production assembly/transport component CsgG / outer membrane-bounded periplasmic space / Prokaryotic membrane lipoprotein lipid attachment site profile. / identical protein binding / plasma membrane / Curli production assembly/transport component CsgG
Function and homology information
Biological speciesEscherichia coli (E. coli) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.96 Å
AuthorsHatstat AK / Melo A / Tse E / Merz GE
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)F32GM147962 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)K99GM155611 United States
CitationJournal: To Be Published
Title: De novo design of semisynthetic protein nanopores
Authors: Schnaider LS / Hatstat AK / Scott AJ / Tan S / Hambley R / Dawson W / Polizzi N / Wallace EJ / Merz GE / DeGrado WF
History
DepositionJul 19, 2025-
Header (metadata) releaseSep 16, 2026-
Map releaseSep 16, 2026-
UpdateSep 16, 2026-
Current statusSep 16, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_71746.png

Downloads & links

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Map

FileDownload / File: emd_71746.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 440 pix.
= 366.96 Å		0.83 Å/pix.
x 440 pix.
= 366.96 Å		0.83 Å/pix.
x 440 pix.
= 366.96 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.834 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-1.1113218 - 2.0559814
Average (Standard dev.)0.00006701286 (±0.047983002)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions440440440
Spacing440440440
CellA=B=C: 366.96 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_71746_additional_1.map
Projections & Slices
AxesZYX

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Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_71746_half_map_1.map
Projections & Slices
AxesZYX

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Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_71746_half_map_2.map
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Sample components

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Entire : Nanopore assembly of CsgG nonamer with CsgX1C nonamer

EntireName: Nanopore assembly of CsgG nonamer with CsgX1C nonamer
Components
  • Complex: Nanopore assembly of CsgG nonamer with CsgX1C nonamer
    • Protein or peptide: CsgX1C
    • Protein or peptide: Curli production assembly/transport component CsgG

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Supramolecule #1: Nanopore assembly of CsgG nonamer with CsgX1C nonamer

SupramoleculeName: Nanopore assembly of CsgG nonamer with CsgX1C nonamer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Escherichia coli (E. coli)

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Macromolecule #1: CsgX1C

MacromoleculeName: CsgX1C / type: protein_or_peptide / ID: 1 / Number of copies: 9 / Enantiomer: LEVO
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 6.210905 KDa
SequenceString:
GTMTFQFRNP NFGGNPNNGA FLLCSAQAQN AGILAAQLWN NGDYDRALSL FIAVVQSC

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Macromolecule #2: Curli production assembly/transport component CsgG

MacromoleculeName: Curli production assembly/transport component CsgG / type: protein_or_peptide / ID: 2 / Number of copies: 9 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli (E. coli)
Molecular weightTheoretical: 30.091146 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: CLTAPPKEAA RPTLMPRAQS YKDLTHLPAP TGKIFVSVYN IQDETGQFKP YPASNQSTAV PQSATAMLVT ALKDSRWFIP LERQGLQNL LNERKIIRAA QENGTVAINN RIPLQSLTAA NIMVEGSIIG YESNVKSGGV GARYFGIGAD TQYQLDQIAV N LRVVNVST ...String:
CLTAPPKEAA RPTLMPRAQS YKDLTHLPAP TGKIFVSVYN IQDETGQFKP YPASNQSTAV PQSATAMLVT ALKDSRWFIP LERQGLQNL LNERKIIRAA QENGTVAINN RIPLQSLTAA NIMVEGSIIG YESNVKSGGV GARYFGIGAD TQYQLDQIAV N LRVVNVST GEILSSVNTS KTILSYEVQA GVFRFIDYQR LLEGEVGYTS NEPVMLCLMS AIETGVIFLI NDGIDRGLWD LQ NKAERQN DILVKYRHMS VPPESSAWSH PQFEK

UniProtKB: Curli production assembly/transport component CsgG

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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

Concentration0.3 mg/mL
BufferpH: 7
GridModel: Quantifoil / Material: GOLD / Mesh: 200 / Support film - Material: GRAPHENE OXIDE / Support film - topology: CONTINUOUS
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) / Average electron dose: 46.0 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: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.96 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC
Details: particle stack parsed for reconstruction (87153 particles) was symmetry expanded with C9 symmetry to afford 784377 particles
Number images used: 784377
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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