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- PDB-7jz3: Osmoporin OmpC from E.coli K12 -

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Database: PDB / ID: 7jz3
TitleOsmoporin OmpC from E.coli K12
ComponentsOuter membrane protein C
KeywordsTRANSPORT PROTEIN / Osmoporin OmpC
Function / homology
Function and homology information

porin activity / pore complex / ion transmembrane transport / cell outer membrane
Porin, Gram-negative type / Porin, gammaproteobacterial / Porin, Gram-negative type, conserved site / Porin domain superfamily / Gram-negative porin
Outer membrane protein C
Biological speciesEscherichia coli (E. coli)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.56 Å
AuthorsLyu, M. / Su, C. / Morgan, C.E. / Bolla, J.R. / Robinson, C.V. / Yu, E.W.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: Nat Methods / Year: 2021
Title: A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins.
Authors: Chih-Chia Su / Meinan Lyu / Christopher E Morgan / Jani Reddy Bolla / Carol V Robinson / Edward W Yu /
Abstract: Single-particle cryo-electron microscopy (cryo-EM) has become a powerful technique in the field of structural biology. However, the inability to reliably produce pure, homogeneous membrane protein ...Single-particle cryo-electron microscopy (cryo-EM) has become a powerful technique in the field of structural biology. However, the inability to reliably produce pure, homogeneous membrane protein samples hampers the progress of their structural determination. Here, we develop a bottom-up iterative method, Build and Retrieve (BaR), that enables the identification and determination of cryo-EM structures of a variety of inner and outer membrane proteins, including membrane protein complexes of different sizes and dimensions, from a heterogeneous, impure protein sample. We also use the BaR methodology to elucidate structural information from Escherichia coli K12 crude membrane and raw lysate. The findings demonstrate that it is possible to solve high-resolution structures of a number of relatively small (<100 kDa) and less abundant (<10%) unidentified membrane proteins within a single, heterogeneous sample. Importantly, these results highlight the potential of cryo-EM for systems structural proteomics.
Validation Report
SummaryFull reportAbout validation report
DepositionSep 1, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 20, 2021Provider: repository / Type: Initial release

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Deposited unit
B: Outer membrane protein C
C: Outer membrane protein C
A: Outer membrane protein C

Theoretical massNumber of molelcules
Total (without water)115,0093

TypeNameSymmetry operationNumber
identity operation1_5551
Buried area9590 Å2
ΔGint-51 kcal/mol
Surface area40980 Å2


#1: Protein Outer membrane protein C

Mass: 38336.242 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: C6K7N1

Experimental details


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

Sample preparation

ComponentName: Osmoporin OmpC / Type: COMPLEX / Entity ID: #1 / Source: NATURAL
Source (natural)Organism: Escherichia coli (E. coli) / Strain: K-12
Buffer solutionpH: 7.5
SpecimenConc.: 0.7 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 40 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)


3D reconstructionResolution: 2.56 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 68628 / Symmetry type: POINT

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