6KCB
Room temperature structure of lysozyme delivered in shortening A by serial millisecond crystallography
Summary for 6KCB
Entry DOI | 10.2210/pdb6kcb/pdb |
Descriptor | Lysozyme C, SODIUM ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | room temperature, serial crystallography, lysozyme, hydrolase |
Biological source | Gallus gallus (Chicken) |
Total number of polymer chains | 1 |
Total formula weight | 16374.55 |
Authors | Nam, K.H. (deposition date: 2019-06-27, release date: 2020-05-20, Last modification date: 2024-10-16) |
Primary citation | Nam, K.H. Shortening injection matrix for serial crystallography. Sci Rep, 10:107-107, 2020 Cited by PubMed Abstract: Serial crystallography allows crystal structures to be determined at room temperature through the steady delivery of crystals to the X-ray interaction point. Viscous delivery media are advantageous because they afford efficient sample delivery from an injector or syringe at a low flow rate. Hydrophobic delivery media, such as lipidic cubic phase (LCP) or grease, provide a stable injection stream and are widely used. The development of new hydrophobic delivery materials can expand opportunities for future SX studies with various samples. Here, I introduce fat-based shortening as a delivery medium for SX experiments. This material is commercially available at low cost and is straightforward to handle because its phase (i.e., solid or liquid) can be controlled by temperature. Shortening was extruded from a syringe needle in a stable injection stream even below 200 nl/min. X-ray exposed shortening produced several background scattering rings, which have similar or lower intensities than those of LCP and contribute negligibly to data processing. Serial millisecond crystallography was performed using two shortening delivery media, and the room temperature crystal structures of lysozyme and glucose isomerase were successfully determined at resolutions of 1.5-2.0 Å. Therefore, shortening can be used as a sample delivery medium in SX experiments. PubMed: 31919476DOI: 10.1038/s41598-019-56135-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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