@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{bodenheimer_meilleur_2016, title={Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states}, volume={590}, ISSN={["1873-3468"]}, DOI={10.1002/1873-3468.12464}, abstractNote={Trichoderma reesei Cel7A efficiently hydrolyses cellulose. We report here the crystallographic structures of the wild‐type TrCel7A catalytic domain (CD) in an open state and, for the first time, in a closed state. Molecular dynamics (MD) simulations indicate that the loops along the CD tunnel move in concerted motions. Together, the crystallographic and MD data suggest that the CD cycles between the tense and relaxed forms that are characteristic of work producing enzymes. Analysis of the interactions formed by R251 provides a structural rationale for the concurrent decrease in product inhibition and catalytic efficiency measured for product‐binding site mutants.}, number={23}, journal={FEBS LETTERS}, publisher={Wiley-Blackwell}, author={Bodenheimer, Annette M. and Meilleur, Flora}, year={2016}, month={Dec}, pages={4429–4438} }
 @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{bodenheimer_cuneo_swartz_he_o'neill_myles_evans_meilleur_section_2014, title={Crystallization and preliminary X-ray diffraction analysis of Hypocrea jecorina Cel7A in two new crystal forms}, volume={70}, ISSN={["2053-230X"]}, url={http://europepmc.org/abstract/med/24915091}, DOI={10.1107/s2053230x14008851}, abstractNote={Cel7A (previously known as cellobiohydrolase I) fromHypocrea jecorinawas crystallized in two crystalline forms, neither of which have been previously reported. Both forms co-crystallize under the same crystallization conditions. The first crystal form belonged to space groupC2, with unit-cell parametersa= 152.5,b= 44.9,c= 57.6 Å, β = 101.2°, and diffracted X-rays to 1.5 Å resolution. The second crystal form belonged to space groupP6322, with unit-cell parametersa=b≃ 155,c≃ 138 Å, and diffracted X-rays to 2.5 Å resolution. The crystals were obtained using full-length Cel7A, which consists of a large 434-residue N-terminal catalytic domain capable of cleaving cellulose, a 27-residue flexible linker and a small 36-residue C-terminal carbohydrate-binding module (CBM). However, a preliminary analysis of the electron-density maps suggests that the linker and CBM are disordered in both crystal forms. Complete refinement and structure analysis are currently in progress.}, number={Pt 6}, journal={ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS}, author={Bodenheimer, A.M. and Cuneo, M.J. and Swartz, P.D. and He, J. and O'Neill, H.M. and Myles, D.A. and Evans, B.R. and Meilleur, Flora and Section, F.}, year={2014}, month={Jun}, pages={773–776} }