@article{william b. o'dell_swartz_weiss_meilleur_2017, title={Crystallization of a fungal lytic polysaccharide monooxygenase expressed from glycoengineered Pichia pastoris for X-ray and neutron diffraction}, volume={73}, ISSN={["2053-230X"]}, DOI={10.1107/s2053230x16020318}, abstractNote={Lytic polysaccharide monooxygenases (LPMOs) are carbohydrate-disrupting enzymes secreted by bacteria and fungi that break glycosidic bondsviaan oxidative mechanism. Fungal LPMOs typically act on cellulose and can enhance the efficiency of cellulose-hydrolyzing enzymes that release soluble sugars for bioethanol production or other industrial uses. The enzyme PMO-2 fromNeurospora crassa(NcPMO-2) was heterologously expressed inPichia pastoristo facilitate crystallographic studies of the fungal LPMO mechanism. Diffraction resolution and crystal morphology were improved by expressingNcPMO-2 from a glycoengineered strain ofP. pastorisand by the use of crystal seeding methods, respectively. These improvements resulted in high-resolution (1.20 Å) X-ray diffraction data collection at 100 K and the production of a largeNcPMO-2 crystal suitable for room-temperature neutron diffraction data collection to 2.12 Å resolution.}, number={2}, journal={ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS}, publisher={International Union of Crystallography (IUCr)}, author={William B. O'Dell and Swartz, Paul D. and Weiss, Kevin L. and Meilleur, Flora}, year={2017}, month={Feb}, pages={70–78} }
 @article{william b. o'dell_agarwal_meilleur_2017, title={Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase}, volume={56}, ISSN={["1521-3773"]}, url={https://doi.org/10.1002/anie.201610502}, DOI={10.1002/anie.201610502}, abstractNote={Abstract}, number={3}, journal={ANGEWANDTE CHEMIE-INTERNATIONAL EDITION}, publisher={Wiley}, author={William B. O'Dell and Agarwal, Pratul K. and Meilleur, Flora}, year={2017}, month={Jan}, pages={767–770} }
 @article{bodenheimer_william b. o'dell_stanley_meilleur_2017, title={Structural studies of Neurospora crassa LPMO9D and redox partner CDHIIA using neutron crystallography and small-angle scattering}, volume={448}, ISSN={["1873-426X"]}, DOI={10.1016/j.carres.2017.03.001}, abstractNote={Sensitivity to hydrogen/deuterium and lack of observable radiation damage makes cold neutrons an ideal probe the structural studies of proteins with highly photosensitive groups such as the copper center of lytic polysaccharide monooxygenases (LPMOs) and flavin adenine dinucleotide (FAD) and heme redox cofactors of cellobiose dehydrogenases (CDHs). Here, neutron crystallography and small-angle neutron scattering are used to investigate Neurospora crassa LPMO9D (NcLPMO9D) and CDHIIA (NcCDHIIA), respectively. The presence of LPMO greatly enhances the efficiency of commercial glycoside hydrolase cocktails in the depolymerization of cellulose. LPMOs can receive electrons from CDHs to activate molecular dioxygen for the oxidation of cellulose resulting in chain cleavage and disruption of local crystallinity. Using neutron protein crystallography, the hydrogen/deuterium atoms of NcLPMO9D could be located throughout the structure. At the copper active site, the protonation states of the side chains of His1, His84, His157 and Tyr168, and the orientation of water molecules could be determined. Small-angle neutron scattering measurements provided low resolution models of NcCDHIIA with both the dehydrogenase and cytochrome domains in oxidized states that exhibited elongated conformations. This work demonstrates the suitability of neutron diffraction and scattering for characterizing enzymes critical to oxidative cellulose deconstruction.}, journal={CARBOHYDRATE RESEARCH}, publisher={Elsevier BV}, author={Bodenheimer, Annette M. and William B. O'Dell and Stanley, Christopher B. and Meilleur, Flora}, year={2017}, month={Aug}, pages={200–204} }
 @article{william b. o'dell_bodenheimer_meilleur_2016, title={Neutron protein crystallography: A complementary tool for locating hydrogens in proteins}, volume={602}, ISSN={["1096-0384"]}, url={https://doi.org/10.1016/j.abb.2015.11.033}, DOI={10.1016/j.abb.2015.11.033}, abstractNote={Neutron protein crystallography is a powerful tool for investigating protein chemistry because it directly locates hydrogen atom positions in a protein structure. The visibility of hydrogen and deuterium atoms arises from the strong interaction of neutrons with the nuclei of these isotopes. Positions can be unambiguously assigned from diffraction at resolutions typical of protein crystals. Neutrons have the additional benefit to structural biology of not inducing radiation damage in protein crystals. The same crystal could be measured multiple times for parametric studies. Here, we review the basic principles of neutron protein crystallography. The information that can be gained from a neutron structure is presented in balance with practical considerations. Methods to produce isotopically-substituted proteins and to grow large crystals are provided in the context of neutron structures reported in the literature. Available instruments for data collection and software for data processing and structure refinement are described along with technique-specific strategies including joint X-ray/neutron structure refinement. Examples are given to illustrate, ultimately, the unique scientific value of neutron protein crystal structures.}, journal={ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS}, publisher={Elsevier BV}, author={William B. O'Dell and Bodenheimer, Annette M. and Meilleur, Flora}, year={2016}, month={Jul}, pages={48–60} }
 @article{busch_pardo_o'dell_bruce_lorenz_mclain_2013, title={On the structure of water and chloride ion interactions with a peptide backbone in solution}, volume={15}, number={48}, journal={Physical Chemistry Chemical Physics}, author={Busch, S. and Pardo, L. C. and O'Dell, W. B. and Bruce, C. D. and Lorenz, C. D. and McLain, S. E.}, year={2013}, pages={21023–21033} }