8AF7
Room temperature SSX crystal structure of CTX-M-14 (10K dataset)
Summary for 8AF7
Entry DOI | 10.2210/pdb8af7/pdb |
Descriptor | Beta-lactamase, SULFATE ION (3 entities in total) |
Functional Keywords | beta-lactamase, serial crystallography, ssx, tapedrive, hydrolase |
Biological source | Klebsiella pneumoniae |
Total number of polymer chains | 1 |
Total formula weight | 27867.38 |
Authors | Oberthuer, D.,Perbandt, M.,Prester, A.,Rohde, H.,Betzel, C.,Yefanov, O. (deposition date: 2022-07-15, release date: 2022-11-16, Last modification date: 2024-04-03) |
Primary citation | Zielinski, K.A.,Prester, A.,Andaleeb, H.,Bui, S.,Yefanov, O.,Catapano, L.,Henkel, A.,Wiedorn, M.O.,Lorbeer, O.,Crosas, E.,Meyer, J.,Mariani, V.,Domaracky, M.,White, T.A.,Fleckenstein, H.,Sarrou, I.,Werner, N.,Betzel, C.,Rohde, H.,Aepfelbacher, M.,Chapman, H.N.,Perbandt, M.,Steiner, R.A.,Oberthuer, D. Rapid and efficient room-temperature serial synchrotron crystallography using the CFEL TapeDrive. Iucrj, 9:778-791, 2022 Cited by PubMed Abstract: Serial crystallography at conventional synchrotron light sources (SSX) offers the possibility to routinely collect data at room temperature using micrometre-sized crystals of biological macromolecules. However, SSX data collection is not yet as routine and currently takes significantly longer than the standard rotation series cryo-crystallography. Thus, its use for high-throughput approaches, such as fragment-based drug screening, where the possibility to measure at physio-logical temperatures would be a great benefit, is impaired. On the way to high-throughput SSX using a conveyor belt based sample delivery system - the CFEL TapeDrive - with three different proteins of biological relevance ( CTX-M-14 β-lactamase, xylanase GH11 and urate oxidase), it is shown here that complete datasets can be collected in less than a minute and only minimal amounts of sample are required. PubMed: 36381150DOI: 10.1107/S2052252522010193 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
Download full validation report