6R7M
Tobacco Mosaic Virus (TMV)
Summary for 6R7M
| Entry DOI | 10.2210/pdb6r7m/pdb |
| EMDB information | 4628 |
| Descriptor | Capsid protein (1 entity in total) |
| Functional Keywords | tobacco, mosaic, virus, tmv, cryo-em, cryowriter, microfluidic |
| Biological source | Tobacco mosaic virus |
| Total number of polymer chains | 1 |
| Total formula weight | 17092.00 |
| Authors | Schmidli, C.,Albiez, S.,Rima, L.,Righetto, R.,Mohammed, I.,Oliva, P.,Kovacik, L.,Stahlberg, H.,Braun, T. (deposition date: 2019-03-29, release date: 2019-07-03, Last modification date: 2024-05-15) |
| Primary citation | Schmidli, C.,Albiez, S.,Rima, L.,Righetto, R.,Mohammed, I.,Oliva, P.,Kovacik, L.,Stahlberg, H.,Braun, T. Microfluidic protein isolation and sample preparation for high-resolution cryo-EM. Proc.Natl.Acad.Sci.USA, 116:15007-15012, 2019 Cited by PubMed Abstract: High-resolution structural information is essential to understand protein function. Protein-structure determination needs a considerable amount of protein, which can be challenging to produce, often involving harsh and lengthy procedures. In contrast, the several thousand to a few million protein particles required for structure determination by cryogenic electron microscopy (cryo-EM) can be provided by miniaturized systems. Here, we present a microfluidic method for the rapid isolation of a target protein and its direct preparation for cryo-EM. Less than 1 μL of cell lysate is required as starting material to solve the atomic structure of the untagged, endogenous human 20S proteasome. Our work paves the way for high-throughput structure determination of proteins from minimal amounts of cell lysate and opens more opportunities for the isolation of sensitive, endogenous protein complexes. PubMed: 31292253DOI: 10.1073/pnas.1907214116 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.92 Å) |
Structure validation
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