9tou
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Room temperature serial AmpC uncomplexed resting state from PAL-XFEL
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Structural highlights
FunctionAMPC_ECOLI This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. Publication Abstract from PubMedWe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 07:21, 17 June 2026.