|Entry||Database: EMDB / ID: EMD-22529|
|Title||Osmoporin OmpC from E.coli K12|
Outer membrane protein C
|Function / homology||Porin, Gram-negative type / Porin, gammaproteobacterial / Porin, Gram-negative type, conserved site / Porin domain superfamily / porin activity / pore complex / ion transmembrane transport / cell outer membrane / Outer membrane protein C|
Function and homology information
|Biological species||Escherichia coli (E. coli)|
|Method||single particle reconstruction / cryo EM / Resolution: 2.56 Å|
|Authors||Lyu M / Su C / Morgan CE / Bolla JR / Robinson CV / Yu EW|
|Funding support|| United States, 1 items |
|Citation||Journal: 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||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_22529.map.gz / Format: CCP4 / Size: 6.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
generated in cubic-lattice coordinate
|Voxel size||X=Y=Z: 1.08 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Additional map: #1
-Entire Osmoporin OmpC
|Entire||Name: Osmoporin OmpC / Number of components: 2|
-Component #1: protein, Osmoporin OmpC
|Protein||Name: Osmoporin OmpC / Recombinant expression: No|
|Source||Species: Escherichia coli (E. coli) / Strain: K-12|
-Component #2: protein, Outer membrane protein C
|Protein||Name: Outer membrane protein C / Number of Copies: 3 / Recombinant expression: No|
|Mass||Theoretical: 38.336242 kDa|
|Source||Species: Escherichia coli (E. coli) / Strain: K-12|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||Specimen conc.: 0.7 mg/mL / pH: 7.5|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 40 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Processing||Method: single particle reconstruction / Number of projections: 68628|
|3D reconstruction||Resolution: 2.56 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
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