7N2K
MicroED structure of sequence variant of repeat segment of the yeast prion New1p phased by ARCIMBOLDO-BORGES
Summary for 7N2K
| Entry DOI | 10.2210/pdb7n2k/pdb |
| Descriptor | prion New1p (2 entities in total) |
| Functional Keywords | amyloid, microed, prion, yeast, new1p, protein fibril |
| Biological source | Saccharomyces cerevisiae |
| Total number of polymer chains | 1 |
| Total formula weight | 814.80 |
| Authors | Flores, M.D.,Richards, L.S.,Zee, C.T.,Glynn, C.,Gallagher-Jones, M.,Sawaya, M.R. (deposition date: 2021-05-29, release date: 2022-06-01, Last modification date: 2024-05-22) |
| Primary citation | Richards, L.S.,Flores, M.D.,Millan, C.,Glynn, C.,Zee, C.T.,Sawaya, M.R.,Gallagher-Jones, M.,Borges, R.J.,Uson, I.,Rodriguez, J.A. Fragment-Based Ab Initio Phasing of Peptidic Nanocrystals by MicroED. Acs Bio Med Chem Au, 3:201-210, 2023 Cited by PubMed Abstract: Electron diffraction (MicroED/3DED) can render the three-dimensional atomic structures of molecules from previously unamenable samples. The approach has been particularly transformative for peptidic structures, where MicroED has revealed novel structures of naturally occurring peptides, synthetic protein fragments, and peptide-based natural products. Despite its transformative potential, MicroED is beholden to the crystallographic phase problem, which challenges its determination of structures. ARCIMBOLDO, an automated, fragment-based approach to structure determination, eliminates the need for atomic resolution, instead enforcing stereochemical constraints through libraries of small model fragments, and discerning congruent motifs in solution space to ensure validation. This approach expands the reach of MicroED to presently inaccessible peptide structures including fragments of human amyloids, and yeast and mammalian prions. For electron diffraction, fragment-based phasing portends a more general phasing solution with limited model bias for a wider set of chemical structures. PubMed: 37096030DOI: 10.1021/acsbiomedchemau.2c00082 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (1.301 Å) |
Structure validation
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