7C09
Structure of lysozyme obtained in SSRF using serial crystallography
Summary for 7C09
| Entry DOI | 10.2210/pdb7c09/pdb |
| Descriptor | Lysozyme C (2 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 14331.16 |
| Authors | Zhao, F.Z. (deposition date: 2020-04-30, release date: 2020-12-09, Last modification date: 2024-10-23) |
| Primary citation | Zhao, F.Z.,Sun, B.,Yu, L.,Xiao, Q.J.,Wang, Z.J.,Chen, L.L.,Liang, H.,Wang, Q.S.,He, J.H.,Yin, D.C. A novel sample delivery system based on circular motion for in situ serial synchrotron crystallography. Lab Chip, 20:3888-3898, 2020 Cited by PubMed Abstract: A sample delivery system is one of the key parts of serial crystallography. It is the main limiting factor affecting the application of serial crystallography. At present, although a variety of useful sample delivery systems have been developed for serial crystallography, it still remains the focus of the field to further improve the performance and efficiency of sample delivery. In existing sample delivery technologies, samples are usually delivered in linear motion. Here we show that the samples can also be delivered using circular motion, which is a novel motion mode never tested before. In this paper, we report a microfluidic rotating-target sample delivery device, which is characterized by the circular motion of the samples, and verify the performance of the device at a synchrotron radiation facility. The microfluidic rotating-target sample delivery device consists of two parts: a microfluidic sample plate and a motion control system. Sample delivery is realized by rotating the microfluidic sample plate containing in situ grown crystals. This device offers significant advantages, including a very wide adjustable range of delivery speed, low background noise, and low sample consumption. Using the microfluidic rotating-target device, we carried out in situ serial crystallography experiments with lysozyme and proteinase K as model samples at the Shanghai Synchrotron Radiation Facility, and performed structural determination based on the serial crystallographic data. The results showed that the designed device is fully compatible with the synchrotron radiation facility, and the structure determination of proteins is successful using the serial crystallographic data obtained with the device. PubMed: 32966481DOI: 10.1039/d0lc00443j PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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