6HU5
STRUCTURE OF HEWL BY ELECTRON DIFFRACTION AND MICROFOCUS DIFFRACTION
Summary for 6HU5
| Entry DOI | 10.2210/pdb6hu5/pdb |
| Related | 1LCN 1LKR 3J6K 5A3E 5K7O 5O4W 5OCV 6HT2 |
| Descriptor | Lysozyme C, CHLORIDE ION (2 entities in total) |
| Functional Keywords | lysozyme, hewl, ed, electron, diffraction, hydrolase, crystal, chloride, halogen, protein, dimer, microfocus |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 2 |
| Total formula weight | 28768.68 |
| Authors | Garau, G. (deposition date: 2018-10-05, release date: 2019-01-23, Last modification date: 2024-11-13) |
| Primary citation | Lanza, A.,Margheritis, E.,Mugnaioli, E.,Cappello, V.,Garau, G.,Gemmi, M. Nanobeam precession-assisted 3D electron diffraction reveals a new polymorph of hen egg-white lysozyme. Iucrj, 6:178-188, 2019 Cited by PubMed Abstract: Recent advances in 3D electron diffraction have allowed the structure determination of several model proteins from submicrometric crystals, the unit-cell parameters and structures of which could be immediately validated by known models previously obtained by X-ray crystallography. Here, the first new protein structure determined by 3D electron diffraction data is presented: a previously unobserved polymorph of hen egg-white lysozyme. This form, with unit-cell parameters = 31.9, = 54.4, = 71.8 Å, β = 98.8°, grows as needle-shaped submicrometric crystals simply by vapor diffusion starting from previously reported crystallization conditions. Remarkably, the data were collected using a low-dose stepwise experimental setup consisting of a precession-assisted nanobeam of ∼150 nm, which has never previously been applied for solving protein structures. The crystal structure was additionally validated using X-ray synchrotron-radiation sources by both powder diffraction and single-crystal micro-diffraction. 3D electron diffraction can be used for the structural characterization of submicrometric macromolecular crystals and is able to identify novel protein polymorphs that are hardly visible in conventional X-ray diffraction experiments. Additionally, the analysis, which was performed on both nanocrystals and microcrystals from the same crystallization drop, suggests that an integrated view from 3D electron diffraction and X-ray microfocus diffraction can be applied to obtain insights into the molecular dynamics during protein crystal growth. PubMed: 30867915DOI: 10.1107/S2052252518017657 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (2.8 Å) |
Structure validation
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