11ZN
Structure of peptide segment KLVFFA from amyloid-beta determined by MicroED under cryogenic temperatures
Summary for 11ZN
| Entry DOI | 10.2210/pdb11zn/pdb |
| Descriptor | LYS-LEU-VAL-PHE-PHE-ALA (2 entities in total) |
| Functional Keywords | peptide segment klvffa from amyloid-beta, protein fibril |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 724.91 |
| Authors | |
| Primary citation | Vlahakis, N.W.,Konieczny, K.,Flowers, C.W.,Garcia-Garibay, M.A.,Rodriguez, J.A. Room Temperature Structures of Solvated Organic Molecules Enabled by Liquid Cell Electron Diffraction. Acs Cent.Sci., 12:1592-1600, 2026 Cited by PubMed Abstract: Electron diffraction (MicroED/3DED) enables atomic structure determination from nano- or microcrystals, including dry crystalline powders or mixtures. However, radiation damage and instrument vacuum can limit the interrogation of molecular crystals in solution at room temperature. We now present a strategy for room-temperature MicroED of organic molecular microcrystals suspended in solution, using simple liquid cells: grid sandwiches comprised of two continuous carbon grids that when pressed retain a thin liquid layer between them. In this setting, we find that some room-temperature, hydrated microcrystals are particularly prone to electron beam radiation damage, requiring fast, low dose data collection schemes, direct electron detectors, and multi-crystal data collection. These approaches minimize damage of crystals in liquid cells and facilitate structures at sub-Ångstrom resolution. This tactic enables study of molecular conformations and crystalline phases that may only be accessible in a room-temperature solvated state. PubMed: 42964980DOI: 10.1021/acscentsci.6c00603 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (1.5 Å) |
Structure validation
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