5K2G
Structure of GNNQQNY from yeast prion Sup35 in space group P21 determined by MicroED
Summary for 5K2G
| Entry DOI | 10.2210/pdb5k2g/pdb |
| Related | 5K2E 5K2F 5K2H |
| EMDB information | 8196 8197 8198 8199 |
| Descriptor | Eukaryotic peptide chain release factor GTP-binding subunit (2 entities in total) |
| Functional Keywords | amyloid, yeast prion, protein fibril |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 836.81 |
| Authors | Rodriguez, J.A.,Sawaya, M.R.,Cascio, D.,Eisenberg, D.S. (deposition date: 2016-05-18, release date: 2016-09-14, Last modification date: 2024-03-06) |
| Primary citation | Sawaya, M.R.,Rodriguez, J.,Cascio, D.,Collazo, M.J.,Shi, D.,Reyes, F.E.,Hattne, J.,Gonen, T.,Eisenberg, D.S. Ab initio structure determination from prion nanocrystals at atomic resolution by MicroED. Proc.Natl.Acad.Sci.USA, 113:11232-11236, 2016 Cited by PubMed Abstract: Electrons, because of their strong interaction with matter, produce high-resolution diffraction patterns from tiny 3D crystals only a few hundred nanometers thick in a frozen-hydrated state. This discovery offers the prospect of facile structure determination of complex biological macromolecules, which cannot be coaxed to form crystals large enough for conventional crystallography or cannot easily be produced in sufficient quantities. Two potential obstacles stand in the way. The first is a phenomenon known as dynamical scattering, in which multiple scattering events scramble the recorded electron diffraction intensities so that they are no longer informative of the crystallized molecule. The second obstacle is the lack of a proven means of de novo phase determination, as is required if the molecule crystallized is insufficiently similar to one that has been previously determined. We show with four structures of the amyloid core of the Sup35 prion protein that, if the diffraction resolution is high enough, sufficiently accurate phases can be obtained by direct methods with the cryo-EM method microelectron diffraction (MicroED), just as in X-ray diffraction. The success of these four experiments dispels the concern that dynamical scattering is an obstacle to ab initio phasing by MicroED and suggests that structures of novel macromolecules can also be determined by direct methods. PubMed: 27647903DOI: 10.1073/pnas.1606287113 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (1.1 Å) |
Structure validation
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