7K3M
Crystal Structure of the Beta Lactamase Class D from Chitinophaga pinensis by Serial Crystallography
Summary for 7K3M
| Entry DOI | 10.2210/pdb7k3m/pdb |
| Descriptor | Beta-lactamase (2 entities in total) |
| Functional Keywords | beta lactamase class d, serial crystallography, structural genomics, center for structural genomics of infectious diseases, hydrolase, csgid |
| Biological source | Chitinophaga pinensis DSM 2588 |
| Total number of polymer chains | 1 |
| Total formula weight | 29880.25 |
| Authors | Kim, Y.,Sherrell, D.A.,Johnson, J.,Lavens, A.,Maltseva, N.,Endres, M.,Babnigg, G.,Joachimiak, A.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2020-09-11, release date: 2020-09-23, Last modification date: 2026-03-25) |
| Primary citation | Sherrell, D.A.,Lavens, A.,Wilamowski, M.,Kim, Y.,Chard, R.,Lazarski, K.,Rosenbaum, G.,Vescovi, R.,Johnson, J.L.,Akins, C.,Chang, C.,Michalska, K.,Babnigg, G.,Foster, I.,Joachimiak, A. Fixed-target serial crystallography at the Structural Biology Center. J.Synchrotron Radiat., 29:1141-1151, 2022 Cited by PubMed Abstract: Serial synchrotron crystallography enables the study of protein structures under physiological temperature and reduced radiation damage by collection of data from thousands of crystals. The Structural Biology Center at Sector 19 of the Advanced Photon Source has implemented a fixed-target approach with a new 3D-printed mesh-holder optimized for sample handling. The holder immobilizes a crystal suspension or droplet emulsion on a nylon mesh, trapping and sealing a near-monolayer of crystals in its mother liquor between two thin Mylar films. Data can be rapidly collected in scan mode and analyzed in near real-time using piezoelectric linear stages assembled in an XYZ arrangement, controlled with a graphical user interface and analyzed using a high-performance computing pipeline. Here, the system was applied to two β-lactamases: a class D serine β-lactamase from Chitinophaga pinensis DSM 2588 and L1 metallo-β-lactamase from Stenotrophomonas maltophilia K279a. PubMed: 36073872DOI: 10.1107/S1600577522007895 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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