9TOO
Contaminated room temperature serial crystal structure of CTX-M-15 class A beta-lactamase, drop on fixed target at DLS, 2.6 s mixed with 200 mM avibactam
Summary for 9TOO
| Entry DOI | 10.2210/pdb9too/pdb |
| Descriptor | Beta-lactamase, (2S,5R)-1-formyl-5-[(sulfooxy)amino]piperidine-2-carboxamide, (2S,5R)-7-oxo-6-(sulfooxy)-1,6-diazabicyclo[3.2.1]octane-2-carboxamide, ... (6 entities in total) |
| Functional Keywords | antibiotic resistance, beta-lactamase, inhibitor, dynamics, tr-ssx, antimicrobial protein |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 1 |
| Total formula weight | 28906.93 |
| Authors | Parkinson, L.,Tooke, C.L.,Hinchliffe, P.,Beer, M.,Kamps, J.A.G.,Spencer, J. (deposition date: 2025-12-17, release date: 2026-06-17) |
| Primary citation | Kamps, J.J.A.G.,Hinchliffe, P.,Glerup, J.,Freeman, E.I.,Lang, P.A.,Tooke, C.L.,Beer, M.,Parkinson, L.,Gu, D.H.,Park, S.,Devenish, N.,Zhou, T.,Shilova, A.,Kaur, S.,Rabe, P.,Schofield, C.J.,Spencer, J.,Park, J.,Owen, R.L.,Orville, A.M.,Aller, P. Drop-on-fixed-target reaction initiation approach for serial and time-resolved crystallography. Iucrj, 2026 Cited by PubMed Abstract: We describe the design and implementation of a drop-on-fixed-target method for time-resolved serial crystallography at both synchrotron and XFEL facilities. A piezoelectric droplet dispensing pipette is employed for addition of picolitre volume aqueous droplets (∼40-90 pl; ∼40-55 µm diameter sphere), containing (co-)substrate(s) or ligand(s), onto enzyme microcrystals previously loaded into the trapezoidal wells of an etched crystalline silicon fixed-target chip containing 25 600 wells in a high-density, square grid with 125 µm centre-to-centre well spacing. These features demand exquisite accuracy and thereby constrain motion controls to enable robust time-resolved crystallographic studies. The system was tested with three enzyme systems, comprising lysozyme and two β-lactamases, CTX-M-15 and AmpC. Mitigation strategies for cross-well contamination, including the implementation of interleaved controls, are described; the overall performance of the system at synchrotron and X-ray free-electron laser facilities was evaluated. This drop-on-fixed-target method is a reliable framework for time-resolved crystallography and will improve the consistency of measurements across facilities. PubMed: 42246252DOI: 10.1107/S2052252526003489 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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