7WUC
Room-temperature structure of lysozyme by serial femtosecond crystallography (BITS)
Summary for 7WUC
| Entry DOI | 10.2210/pdb7wuc/pdb |
| Descriptor | Lysozyme C (2 entities in total) |
| Functional Keywords | serial crystallography, serial femtosecond crystallography, room temperature, lysozyme, hydrolase |
| Biological source | Gallus gallus (chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 14331.16 |
| Authors | Nam, K.H. (deposition date: 2022-02-08, release date: 2022-03-02, Last modification date: 2024-11-20) |
| Primary citation | Lee, K.,Kim, J.,Baek, S.,Park, J.,Park, S.,Lee, J.L.,Chung, W.K.,Cho, Y.,Nam, K.H. Combination of an inject-and-transfer system for serial femtosecond crystallography. J.Appl.Crystallogr., 55:813-822, 2022 Cited by PubMed Abstract: Serial femtosecond crystallography (SFX) enables the determination of room-temperature crystal structures of macromolecules with minimized radiation damage and provides time-resolved molecular dynamics by pump-probe or mix-and-inject experiments. In SFX, a variety of sample delivery methods with unique advantages have been developed and applied. The combination of existing sample delivery methods can enable a new approach to SFX data collection that combines the advantages of the individual methods. This study introduces a combined inject-and-transfer system (BITS) method for sample delivery in SFX experiments: a hybrid injection and fixed-target scanning method. BITS allows for solution samples to be reliably deposited on ultraviolet ozone (UVO)-treated polyimide films, at a minimum flow rate of 0.5 nl min, in both vertical and horizontal scanning modes. To utilize BITS in SFX experiments, lysozyme crystal samples were embedded in a viscous lard medium and injected at flow rates of 50-100 nl min through a syringe needle onto a UVO-treated polyimide film, which was mounted on a fixed-target scan stage. The crystal samples deposited on the film were raster scanned with an X-ray free electron laser using a motion stage in both horizontal and vertical directions. Using the BITS method, the room-temperature structure of lysozyme was successfully determined at a resolution of 2.1 Å, and thus BITS could be utilized in future SFX experiments. PubMed: 35979068DOI: 10.1107/S1600576722005556 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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