8CL5
Lysozyme in matrix of lipidic cubic phase of monoolein (LCP)
Summary for 8CL5
| Entry DOI | 10.2210/pdb8cl5/pdb |
| Descriptor | LYSOZYME, Chain A, 1,2-ETHANEDIOL, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | lysozyme, lysozyme activity, catalytic activity, hydrolase activity, hydrolase |
| Biological source | Asplenium bulbiferum subsp. bulbiferum |
| Total number of polymer chains | 1 |
| Total formula weight | 14748.39 |
| Authors | Bertrand, Q.,Kepa, M.W.,Weinert, T.,Wranik, M.,Standfuss, J. (deposition date: 2023-02-16, release date: 2023-12-13, Last modification date: 2024-11-20) |
| Primary citation | Wranik, M.,Kepa, M.W.,Beale, E.V.,James, D.,Bertrand, Q.,Weinert, T.,Furrer, A.,Glover, H.,Gashi, D.,Carrillo, M.,Kondo, Y.,Stipp, R.T.,Khusainov, G.,Nass, K.,Ozerov, D.,Cirelli, C.,Johnson, P.J.M.,Dworkowski, F.,Beale, J.H.,Stubbs, S.,Zamofing, T.,Schneider, M.,Krauskopf, K.,Gao, L.,Thorn-Seshold, O.,Bostedt, C.,Bacellar, C.,Steinmetz, M.O.,Milne, C.,Standfuss, J. A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers. Nat Commun, 14:7956-7956, 2023 Cited by PubMed Abstract: Serial crystallography at X-ray free-electron lasers (XFELs) permits the determination of radiation-damage free static as well as time-resolved protein structures at room temperature. Efficient sample delivery is a key factor for such experiments. Here, we describe a multi-reservoir, high viscosity extruder as a step towards automation of sample delivery at XFELs. Compared to a standard single extruder, sample exchange time was halved and the workload of users was greatly reduced. In-built temperature control of samples facilitated optimal extrusion and supported sample stability. After commissioning the device with lysozyme crystals, we collected time-resolved data using crystals of a membrane-bound, light-driven sodium pump. Static data were also collected from the soluble protein tubulin that was soaked with a series of small molecule drugs. Using these data, we identify low occupancy (as little as 30%) ligands using a minimal amount of data from a serial crystallography experiment, a result that could be exploited for structure-based drug design. PubMed: 38042952DOI: 10.1038/s41467-023-43523-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.31 Å) |
Structure validation
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