9id0

XFEL structure of hNQO1 mixed with NADH in a folded orientation at 300 ms

spinqualitylabelsall models 9id0, resolution 2.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9id0 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.51Å Ligands: ACT, FAD, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NQO1_HUMAN The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Publication Abstract from PubMed Sample consumption for serial femtosecond crystallography with X-ray free electron lasers remains a major limitation preventing broader use in macromolecular crystallography. This drawback is exacerbated in time-resolved (TR) experiments, where the amount of sample required per reaction time point is multiplied by the number of time points investigated. To reduce this limitation, we demonstrate a segmented droplet generation strategy coupled to a mix-and-inject approach for TR studies at the European XFEL. The injector produces synchronized droplet trains that enable stable and reproducible injection of protein crystal slurries at significantly reduced flow rates. Using the human flavoenzyme NAD(P)H:quinone oxidoreductase 1 (NQO1) as a test system, we collected diffraction data after mixing with NADH at 0.3 s and 1.2 s delays. The segmented injection approach achieved up to 97% reduction in sample consumption compared with continuous-flow injection while maintaining data quality suitable for TR crystallography. Reproducible electron density features consistent with low-occupancy NADH binding illustrate both the feasibility and the current limits of studying dynamic redox enzymes using this approach. This work establishes segmented droplet generation as a sample-efficient and XFEL-compatible method for future time-resolved serial crystallography experiments. Minimized sample consumption for time-resolved serial crystallography applied to the redox cycle of human NQO1.,Doppler D, Grieco A, Koh D, Manna A, Ansari A, Alvarez R, Karpos K, Le H, Sonker M, Ketawala GK, Mahmud S, Quereda-Moraleda I, Sen S, Pey AL, Letrun R, Dorner K, Koliyadu JCP, de Wijn R, Bielecki J, Han H, Kim C, Koua FHM, Round A, Sarma A, Sato T, Schmidt C, Vakili M, Zabelskii D, Bean R, Mancuso AP, Schulz J, Fromme R, Medina M, Grant TD, Fromme P, Kirian RA, Botha S, Manuel Martin-Garcia J, Ros A Commun Chem. 2026 Jan 29. doi: 10.1038/s42004-026-01908-9. PMID:41611948 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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