Jennifer A Doebbler

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Rhodobacter capsulatus xanthine dehydrogenase (XDH) is an (alphabeta)(2) heterotetrameric cytoplasmic enzyme that resembles eukaryotic xanthine oxidoreductases in respect to both amino acid sequence and structural fold. To obtain a detailed understanding of the mechanism of substrate and inhibitor binding at the active site, we solved crystal structures of(More)
Analyses combining X-ray powder diffraction (XRD) and solid-state NMR (SSNMR) data can now provide crystal structures in challenging powders that are inaccessible by traditional methods. The flavonoid catechin is an ideal candidate for these methods, as it has eluded crystallographic characterization despite extensive study. Catechin was first described(More)
Macromolecular structures can be solved via molecular replacement from powder diffraction data collected not only on multi-analyzer diffractometers but also on image plates. Diffraction peaks recorded on image plates are generally broader than those collected using an array of crystal analyzer detectors, but the image-plate data often allow the use of(More)
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