7WB9
Crystal structure of Bovine Pancreatic Trypsin in complex with 5-Chlorotryptamine at Room Temperature
Summary for 7WB9
| Entry DOI | 10.2210/pdb7wb9/pdb |
| Descriptor | Cationic trypsin, 2-(5-chloranyl-1~{H}-indol-3-yl)ethanamine, DIMETHYL SULFOXIDE, ... (5 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 23637.16 |
| Authors | Sakai, N.,Okumura, H.,Yamamoto, M.,Kumasaka, T. (deposition date: 2021-12-15, release date: 2022-06-15, Last modification date: 2024-11-06) |
| Primary citation | Okumura, H.,Sakai, N.,Murakami, H.,Mizuno, N.,Nakamura, Y.,Ueno, G.,Masunaga, T.,Kawamura, T.,Baba, S.,Hasegawa, K.,Yamamoto, M.,Kumasaka, T. In situ crystal data-collection and ligand-screening system at SPring-8. Acta Crystallogr.,Sect.F, 78:241-251, 2022 Cited by PubMed Abstract: In situ diffraction data collection using crystallization plates has been utilized for macromolecules to evaluate crystal quality without requiring additional sample treatment such as cryocooling. Although it is difficult to collect complete data sets using this technique due to the mechanical limitation of crystal rotation, recent advances in methods for data collection from multiple crystals have overcome this issue. At SPring-8, an in situ diffraction measurement system was constructed consisting of a goniometer for a plate, an articulated robot and plate storage. Using this system, complete data sets were obtained utilizing the small-wedge measurement method. Combining this system with an acoustic liquid handler to prepare protein-ligand complex crystals by applying fragment compounds to trypsin crystals for in situ soaking, binding was confirmed for seven out of eight compounds. These results show that the system functioned properly to collect complete data for structural analysis and to expand the capability for ligand screening in combination with a liquid dispenser. PubMed: 35647681DOI: 10.1107/S2053230X22005283 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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