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-Structure paper
Title | Cryo-EM and solid state NMR together provide a more comprehensive structural investigation of protein fibrils. |
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Journal, issue, pages | Protein Sci, Vol. 33, Issue 10, Page e5168, Year 2024 |
Publish date | Sep 14, 2024 |
Authors | Blake D Fonda / Masato Kato / Yang Li / Dylan T Murray / |
PubMed Abstract | The tropomyosin 1 isoform I/C C-terminal domain (Tm1-LC) fibril structure is studied jointly with cryogenic electron microscopy (cryo-EM) and solid state nuclear magnetic resonance (NMR). This study ...The tropomyosin 1 isoform I/C C-terminal domain (Tm1-LC) fibril structure is studied jointly with cryogenic electron microscopy (cryo-EM) and solid state nuclear magnetic resonance (NMR). This study demonstrates the complementary nature of these two structural biology techniques. Chemical shift assignments from solid state NMR are used to determine the secondary structure at the level of individual amino acids, which is faithfully seen in cryo-EM reconstructions. Additionally, solid state NMR demonstrates that the region not observed in the reconstructed cryo-EM density is primarily in a highly mobile random coil conformation rather than adopting multiple rigid conformations. Overall, this study illustrates the benefit of investigations combining cryo-EM and solid state NMR to investigate protein fibril structure. |
External links | Protein Sci / PubMed:39276003 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 2.31 Å |
Structure data | EMDB-45130, PDB-9c1u: |
Source |
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Keywords | PROTEIN FIBRIL |