5VY5
Rabbit muscle aldolase using 200keV
Summary for 5VY5
| Entry DOI | 10.2210/pdb5vy5/pdb |
| EMDB information | 8743 |
| Descriptor | Fructose-bisphosphate aldolase A (1 entity in total) |
| Functional Keywords | glycolytic enzyme, lyase |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 4 |
| Total formula weight | 157054.69 |
| Authors | Herzik Jr., M.A.,Wu, M.,Lander, G.C. (deposition date: 2017-05-24, release date: 2017-06-14, Last modification date: 2024-03-13) |
| Primary citation | Herzik, M.A.,Wu, M.,Lander, G.C. Achieving better-than-3- angstrom resolution by single-particle cryo-EM at 200 keV. Nat. Methods, 14:1075-1078, 2017 Cited by PubMed Abstract: Nearly all single-particle cryo-EM structures resolved to better than 4-Å resolution have been determined using 300-keV transmission electron microscopes (TEMs). We demonstrate that it is possible to obtain reconstructions of macromolecular complexes of different sizes to better than 3-Å resolution using a 200-keV TEM. These structures are of sufficient quality to unambiguously assign amino acid rotameric conformations and identify ordered water molecules. PubMed: 28991891DOI: 10.1038/nmeth.4461 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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