9BDJ
MicroED structure of bovine liver catalase with missing cone eliminated by suspended drop
Summary for 9BDJ
| Entry DOI | 10.2210/pdb9bdj/pdb |
| EMDB information | 44453 |
| Descriptor | Catalase, PROTOPORPHYRIN IX CONTAINING FE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | heme-containing enzyme, oxidoreductase |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 4 |
| Total formula weight | 245444.27 |
| Authors | Gillman, C.,Bu, G.,Gonen, T. (deposition date: 2024-04-11, release date: 2024-09-18, Last modification date: 2024-10-16) |
| Primary citation | Gillman, C.,Bu, G.,Danelius, E.,Hattne, J.,Nannenga, B.L.,Gonen, T. Eliminating the missing cone challenge through innovative approaches. J Struct Biol X, 9:100102-100102, 2024 Cited by PubMed Abstract: Microcrystal electron diffraction (MicroED) has emerged as a powerful technique for unraveling molecular structures from microcrystals too small for X-ray diffraction. However, a significant hurdle arises with plate-like crystals that consistently orient themselves flat on the electron microscopy grid. If the normal of the plate correlates with the axes of the crystal lattice, the crystal orientations accessible for measurement are restricted because the crystal cannot be arbitrarily rotated. This limits the information that can be acquired, resulting in a missing cone of information. We recently introduced a novel crystallization strategy called suspended drop crystallization and proposed that crystals in a suspended drop could effectively address the challenge of preferred crystal orientation. Here we demonstrate the success of the suspended drop approach in eliminating the missing cone in two samples that crystallize as thin plates: bovine liver catalase and the SARS‑CoV‑2 main protease (Mpro). This innovative solution proves indispensable for crystals exhibiting systematic preferred orientations, unlocking new possibilities for structure determination by MicroED. PubMed: 38962493DOI: 10.1016/j.yjsbx.2024.100102 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (4 Å) |
Structure validation
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