9top

Contaminated room temperature serial crystal structure of CTX-M-15 class A beta-lactamase, drop on fixed target at DLS, 2.6 s 'control' contaminated with avibactam

spinqualitylabelsall models 9top, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9top is a 1 chain structure with sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: CL, FYG, NA, NXL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G3G192_KLEPN Publication Abstract from PubMed 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 ( approximately 40-90 pl; approximately 40-55 microm 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 microm 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 beta-lactamases, CTX-M-15 and AmpC(EC). 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. Drop-on-fixed-target reaction initiation approach for serial and time-resolved crystallography.,Kamps JJAG, Hinchliffe P, Glerup J, Freeman EI, Lang PA, Tooke CL, Beer M, Parkinson L, Gu DH, Park S, Devenish N, Zhou T, Shilova A, Kaur S, Rabe P, Schofield CJ, Spencer J, Park J, Owen RL, Orville AM, Aller P IUCrJ. 2026 Jul 1. doi: 10.1107/S2052252526003489. PMID:42246252 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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