@article{schroder_william b. o'dell_webb_agarwal_meilleur_2022, title={Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase}, volume={11}, ISSN={["2041-6539"]}, url={https://doi.org/10.1039/D2SC05031E}, DOI={10.1039/d2sc05031e}, abstractNote={Superoxo and hydroperoxo intermediates were cryotrapped at the copper active site of lytic polysaccharide monooxygenase using neutron protein crystallography.}, journal={CHEMICAL SCIENCE}, author={Schroder, Gabriela C. and William B. O'Dell and Webb, Simon P. and Agarwal, Pratul K. and Meilleur, Flora}, year={2022}, month={Nov} }
 @article{schroeder_meilleur_2021, title={Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography}, volume={77}, ISSN={["2059-7983"]}, url={https://doi.org/10.1107/S2059798321009025}, DOI={10.1107/S2059798321009025}, abstractNote={Metalloproteins catalyze a range of reactions, with enhanced chemical functionality due to their metal cofactor. The reaction mechanisms of metalloproteins have been experimentally characterized by spectroscopy, macromolecular crystallography and cryo-electron microscopy. An important caveat in structural studies of metalloproteins remains the artefacts that can be introduced by radiation damage. Photoreduction, radiolysis and ionization deriving from the electromagnetic beam used to probe the structure complicate structural and mechanistic interpretation. Neutron protein diffraction remains the only structural probe that leaves protein samples devoid of radiation damage, even when data are collected at room temperature. Additionally, neutron protein crystallography provides information on the positions of light atoms such as hydrogen and deuterium, allowing the characterization of protonation states and hydrogen-bonding networks. Neutron protein crystallography has further been used in conjunction with experimental and computational techniques to gain insight into the structures and reaction mechanisms of several transition-state metal oxidoreductases with iron, copper and manganese cofactors. Here, the contribution of neutron protein crystallography towards elucidating the reaction mechanism of metalloproteins is reviewed.}, number={10}, journal={ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY}, publisher={International Union of Crystallography (IUCr)}, author={Schroeder, Gabriela C. and Meilleur, Flora}, year={2021}, month={Oct}, pages={1251–1269} }
 @article{schroder_william b. o'dell_swartz_meilleur_2021, title={Preliminary results of neutron and X-ray diffraction data collection on a lytic polysaccharide monooxygenase under reduced and acidic conditions}, volume={77}, ISSN={["2053-230X"]}, url={https://doi.org/10.1107/S2053230X21002399}, DOI={10.1107/S2053230X21002399}, abstractNote={Lytic polysaccharide monooxygenases (LPMOs) are copper-center enzymes that are involved in the oxidative cleavage of the glycosidic bond in crystalline cellulose and other polysaccharides. The LPMO reaction is initiated by the addition of a reductant and oxygen to ultimately form an unknown activated copper–oxygen species that is responsible for polysaccharide-substrate H-atom abstraction. Given the sensitivity of metalloproteins to radiation damage, neutron protein crystallography provides a nondestructive technique for structural characterization while also informing on the positions of H atoms. Neutron cryo-crystallography permits the trapping of catalytic intermediates, thereby providing insight into the protonation states and chemical nature of otherwise short-lived species in the reaction mechanism. To characterize the reaction-mechanism intermediates of LPMO9D from Neurospora crassa, a cryo-neutron diffraction data set was collected from an ascorbate-reduced crystal. A second neutron diffraction data set was collected at room temperature from an LPMO9D crystal exposed to low-pH conditions to probe the protonation states of ionizable groups involved in catalysis under acidic conditions.}, number={4}, journal={ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS}, publisher={International Union of Crystallography (IUCr)}, author={Schroder, Gabriela C. and William B. O'Dell and Swartz, Paul D. and Meilleur, Flora}, year={2021}, month={Apr}, pages={128–133} }
 @article{schröder_o?dell_myles_kovalevsky_meilleur_2018, title={IMAGINE: Neutrons reveal enzyme chemistry}, volume={74}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-85051271888&partnerID=MN8TOARS}, DOI={10.1107/S2059798318001626}, abstractNote={Neutron diffraction is exquisitely sensitive to the positions of H atoms in protein crystal structures. IMAGINE is a high-intensity, quasi-Laue neutron crystallography beamline developed at the High Flux Isotope Reactor (HFIR) at Oak Ridge National Laboratory. This state-of-the-art facility for neutron diffraction has enabled detailed structural analysis of macromolecules. IMAGINE is especially suited to resolve individual H atoms in protein structures, enabling neutron protein structures to be determined at or near atomic resolutions from crystals with volumes of less than 1 mm3 and unit-cell edges of less than 150 Å. Beamline features include elliptical focusing mirrors that deliver neutrons into a 2.0 × 3.2 mm focal spot at the sample position, and variable short- and long-wavelength cutoff optics that provide automated exchange between multiple wavelength configurations. This review gives an overview of the IMAGINE beamline at the HFIR, presents examples of the scientific questions being addressed at this beamline, and highlights important findings in enzyme chemistry that have been made using the neutron diffraction capabilities offered by IMAGINE.}, journal={Acta Crystallographica Section D: Structural Biology}, author={Schröder, G.C. and O?Dell, W.B. and Myles, D.A.A. and Kovalevsky, A. and Meilleur, F.}, year={2018}, pages={778–786} }