7DI8
Electron crystallographic structure of Catalase using a direct electron detector at 300 kV
Summary for 7DI8
| Entry DOI | 10.2210/pdb7di8/pdb |
| Descriptor | Catalase, PROTOPORPHYRIN IX CONTAINING FE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | electron 3d crystallography, direct detector, cryo arm, parallem, oxidoreductase |
| Biological source | Bos taurus (Bovine) |
| Total number of polymer chains | 4 |
| Total formula weight | 245444.27 |
| Authors | Takaba, K.,Maki-Yonekura, S.,Yonekura, K. (deposition date: 2020-11-18, release date: 2020-12-09, Last modification date: 2024-03-27) |
| Primary citation | Takaba, K.,Maki-Yonekura, S.,Inoue, S.,Hasegawa, T.,Yonekura, K. Protein and Organic-Molecular Crystallography With 300kV Electrons on a Direct Electron Detector. Front Mol Biosci, 7:612226-612226, 2020 Cited by PubMed Abstract: Electron 3D crystallography can reveal the atomic structure from undersized crystals of various samples owing to the strong scattering power of electrons. Here, a direct electron detector DE64 was tested for small and thin crystals of protein and an organic molecule using a JEOL CRYO ARM 300 electron microscope. The microscope is equipped with a cold-field emission gun operated at an accelerating voltage of 300 kV, quad condenser lenses for parallel illumination, an in-column energy filter, and a stable rotational goniometer stage. Rotational diffraction data were collected in an unsupervised manner from crystals of a heme-binding enzyme catalase and a representative organic semiconductor material Ph-BTBT-C10. The structures were determined by molecular replacement for catalase and by the direct method for Ph-BTBT-C10. The analyses demonstrate that the system works well for electron 3D crystallography of these molecules with less damaging, a smaller point spread, and less noise than using the conventional scintillator-coupled camera. PubMed: 33469549DOI: 10.3389/fmolb.2020.612226 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (3.2 Å) |
Structure validation
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