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| Rekonstruktion mittels Kryo-EM× | Homologiemodellierung× | |
|---|---|---|
| Fachgebiet | Bioinformatik | Bioinformatik |
| Familie | Process / pipeline | Process / pipeline |
| Entstehungsjahr≠ | 1975 | 1993 |
| Urheber≠ | Joachim Frank | Andrej Sali |
| Typ≠ | Image reconstruction pipeline | Comparative structure prediction pipeline |
| Wegweisende Quelle≠ | Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319. DOI ↗ | Sali, A. & Blundell, T. L. (1993). Comparative protein modelling by satisfaction of spatial restraints. Journal of Molecular Biology, 234(3), 779-815. DOI ↗ |
| Aliasnamen≠ | cryo-electron microscopy, cryo-EM, single-particle cryo-EM | comparative modeling, template-based modeling |
| Verwandt≠ | 3 | 4 |
| Zusammenfassung≠ | Cryo-electron microscopy (cryo-EM) determines three-dimensional macromolecular structures at atomic or near-atomic resolution by imaging proteins frozen in vitreous ice. Pioneered by Frank, Henderson, and others, this technique has revolutionized structural biology by enabling visualization of large, non-crystallizable complexes and capturing functional conformational states. | Homology modeling, also called comparative modeling, predicts the three-dimensional structure of a protein using an experimentally-solved structure of a homologous protein as a template. Introduced by Sali and Blundell in 1993, this method exploits the principle that homologous proteins share similar spatial structures despite differing in amino acid sequence. |
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