7N2L
MicroED structure of a mutant mammalian prion segment
7N2L の概要
エントリーDOI | 10.2210/pdb7n2l/pdb |
分子名称 | prion protein (2 entities in total) |
機能のキーワード | prion, microed, amyloid, protein fibril |
由来する生物種 | synthetic construct |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 1141.15 |
構造登録者 | Flores, M.D.,Richards, L.S.,Zee, C.T.,Glynn, C.,Gallagher-Jones, M.,Sawaya, M.R. (登録日: 2021-05-29, 公開日: 2022-06-01, 最終更新日: 2024-05-22) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON CRYSTALLOGRAPHY (0.9 Å) |
構造検証レポート
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