5WR4
Thermolysin, SFX unliganded form with oil-based carrier
Summary for 5WR4
| Entry DOI | 10.2210/pdb5wr4/pdb |
| Related | 5WR2 5WR3 5WR5 5WR6 |
| Descriptor | Thermolysin, ZINC ION, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | x-ray free-electron laser, serial femtosecond crystallography, microcrystal, structure-based drug design, hydrolase |
| Biological source | Geobacillus stearothermophilus |
| Cellular location | Secreted : P43133 |
| Total number of polymer chains | 1 |
| Total formula weight | 34586.06 |
| Authors | Kunishima, N.,Naitow, H.,Matsuura, Y. (deposition date: 2016-11-29, release date: 2017-08-16, Last modification date: 2023-11-08) |
| Primary citation | Naitow, H.,Matsuura, Y.,Tono, K.,Joti, Y.,Kameshima, T.,Hatsui, T.,Yabashi, M.,Tanaka, R.,Tanaka, T.,Sugahara, M.,Kobayashi, J.,Nango, E.,Iwata, S.,Kunishima, N. Protein-ligand complex structure from serial femtosecond crystallography using soaked thermolysin microcrystals and comparison with structures from synchrotron radiation Acta Crystallogr D Struct Biol, 73:702-709, 2017 Cited by PubMed Abstract: Serial femtosecond crystallography (SFX) with an X-ray free-electron laser is used for the structural determination of proteins from a large number of microcrystals at room temperature. To examine the feasibility of pharmaceutical applications of SFX, a ligand-soaking experiment using thermolysin microcrystals has been performed using SFX. The results were compared with those from a conventional experiment with synchrotron radiation (SR) at 100 K. A protein-ligand complex structure was successfully obtained from an SFX experiment using microcrystals soaked with a small-molecule ligand; both oil-based and water-based crystal carriers gave essentially the same results. In a comparison of the SFX and SR structures, clear differences were observed in the unit-cell parameters, in the alternate conformation of side chains, in the degree of water coordination and in the ligand-binding mode. PubMed: 28777085DOI: 10.1107/S2059798317008919 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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