7F8K
Room temperature structure of bacterial copper amine oxidase determined by serial femtosecond crystallography
Summary for 7F8K
| Entry DOI | 10.2210/pdb7f8k/pdb |
| Descriptor | Phenylethylamine oxidase, COPPER (II) ION (3 entities in total) |
| Functional Keywords | topaquinone copper serial femtosecond x-ray crystallography radiation-damage-free, oxidoreductase |
| Biological source | Arthrobacter globiformis |
| Total number of polymer chains | 1 |
| Total formula weight | 70816.29 |
| Authors | Murakawa, T.,Okajima, T. (deposition date: 2021-07-02, release date: 2021-09-08, Last modification date: 2021-10-13) |
| Primary citation | Murakawa, T.,Suzuki, M.,Arima, T.,Sugahara, M.,Tanaka, T.,Tanaka, R.,Iwata, S.,Nango, E.,Tono, K.,Hayashi, H.,Fukui, K.,Yano, T.,Tanizawa, K.,Okajima, T. Microcrystal preparation for serial femtosecond X-ray crystallography of bacterial copper amine oxidase Acta Crystallogr.,Sect.F, 77:356-363, 2021 Cited by PubMed Abstract: Recent advances in serial femtosecond X-ray crystallography (SFX) using X-ray free-electron lasers have paved the way for determining radiation-damage-free protein structures under nonfreezing conditions. However, the large-scale preparation of high-quality microcrystals of uniform size is a prerequisite for SFX, and this has been a barrier to its widespread application. Here, a convenient method for preparing high-quality microcrystals of a bacterial quinoprotein enzyme, copper amine oxidase from Arthrobacter globiformis, is reported. The method consists of the mechanical crushing of large crystals (5-15 mm), seeding the crushed crystals into the enzyme solution and standing for 1 h at an ambient temperature of ∼26°C, leading to the rapid formation of microcrystals with a uniform size of 3-5 µm. The microcrystals diffracted X-rays to a resolution beyond 2.0 Å in SFX measurements at the SPring-8 Angstrom Compact Free Electron Laser facility. The damage-free structure determined at 2.2 Å resolution was essentially identical to that determined previously by cryogenic crystallography using synchrotron X-ray radiation. PubMed: 34605440DOI: 10.1107/S2053230X21008967 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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