Metodebevisregistrering
Cryo-EM Reconstruction
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.
Kilderegistrering
Citater kopieret ordret fra metodens kilderegistrering. Ingen påstandsniveauverifikation er udledt heraf.
Cryo-Electron Microscopy 3D Reconstruction
Taksonomisk metoderegistrering · process-pipeline / bioinformatics
- Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319. · DOI 10.1146/annurev.biophys.31.082901.134202
- Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E., & Downing, K. H. (1990). Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. Journal of Molecular Biology, 213(4), 899-929. · DOI 10.1016/S0022-2836(05)80271-2
- Scheres, S. H. W. (2016). Processing of structurally heterogeneous cryo-EM data in RELION. Methods in Enzymology, 579, 125-157. · DOI 10.1016/bs.mie.2016.04.012
Kuraterede påstande
Påstande gemt i bevis-loggen, hver med sin egen vurdering.
Ingen kuraterede påstande endnu
Denne visning opfinder ikke en påstandsvurdering, når loggen ingen har.
Relaterede metoder
Genereret fra metodegrafen og vist som maskinelt foreslåede relationer — ingen bevispåstand er udledt.