6WTZ
Cryo-EM structure of E. Coli OmpF
Summary for 6WTZ
Entry DOI | 10.2210/pdb6wtz/pdb |
EMDB information | 21900 |
Descriptor | Outer membrane porin F (2 entities in total) |
Functional Keywords | outer membrane porin, omp, ompf, membrane protein |
Biological source | Escherichia coli (strain K12) |
Total number of polymer chains | 3 |
Total formula weight | 118095.13 |
Authors | Morgan, C.E.,Su, C.-C.,Lyu, M.,Yu, E.W. (deposition date: 2020-05-04, release date: 2021-01-20, Last modification date: 2024-03-06) |
Primary citation | Su, C.C.,Lyu, M.,Morgan, C.E.,Bolla, J.R.,Robinson, C.V.,Yu, E.W. A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins. Nat.Methods, 18:69-75, 2021 Cited by PubMed 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 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. PubMed: 33408407DOI: 10.1038/s41592-020-01021-2 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.15 Å) |
Structure validation
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