6K2S
Crystal structure of proteinase K from Engyodontium album
Summary for 6K2S
| Entry DOI | 10.2210/pdb6k2s/pdb |
| Descriptor | Proteinase K, CALCIUM ION, NITRATE ION, ... (4 entities in total) |
| Functional Keywords | xfel, sfx, hydrolase |
| Biological source | Parengyodontium album (Tritirachium album,Engyodontium album) |
| Total number of polymer chains | 1 |
| Total formula weight | 29100.95 |
| Authors | Sugahara, M.,Motomura, K.,Numata, K. (deposition date: 2019-05-15, release date: 2020-05-20, Last modification date: 2025-03-05) |
| Primary citation | Sugahara, M.,Motomura, K.,Suzuki, M.,Masuda, T.,Joti, Y.,Numata, K.,Tono, K.,Yabashi, M.,Ishikawa, T. Viscosity-adjustable grease matrices for serial nanocrystallography. Sci Rep, 10:1371-1371, 2020 Cited by PubMed Abstract: Serial femtosecond crystallography (SFX) has enabled determination of room temperature structures of proteins with minimum radiation damage. A highly viscous grease matrix acting as a crystal carrier for serial sample loading at a low flow rate of ~0.5 μl min was introduced into the beam path of X-ray free-electron laser. This matrix makes it possible to determine the protein structure with a sample consumption of less than 1 mg of the protein. The viscosity of the matrix is an important factor in maintaining a continuous and stable sample column from a nozzle of a high viscosity micro-extrusion injector for serial sample loading. Using conventional commercial grease (an oil-based, viscous agent) with insufficient control of viscosity in a matrix often gives an unexpectedly low viscosity, providing an unstable sample stream, with effects such as curling of the stream. Adjustment of the grease viscosity is extremely difficult since the commercial grease contains unknown compounds, which may act as unexpected inhibitors of proteins. This study introduces two novel grease matrix carriers comprising known compounds with a viscosity higher than that of conventional greases, to determine the proteinase K structure from nano-/microcrystals. PubMed: 31992735DOI: 10.1038/s41598-020-57675-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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