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7DI8

Electron crystallographic structure of Catalase using a direct electron detector at 300 kV

Summary for 7DI8
Entry DOI10.2210/pdb7di8/pdb
DescriptorCatalase, PROTOPORPHYRIN IX CONTAINING FE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
Functional Keywordselectron 3d crystallography, direct detector, cryo arm, parallem, oxidoreductase
Biological sourceBos taurus (Bovine)
Total number of polymer chains4
Total formula weight245444.27
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 citationTakaba, 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: 33469549
DOI: 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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