9tou | pdb_00009tou

Room temperature serial AmpC uncomplexed resting state from PAL-XFEL

spinqualitylabelsall models 9tou, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9tou is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.88Å Ligands: CL, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMPC_ECOLI This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. 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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