Flora Meilleur

Tandrup, T., Lo Leggio, L., & Meilleur, F. (2023). Joint X-ray/neutron structure of Lentinus similis AA9_A at room temperature. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 79, 1–7. https://doi.org/10.1107/S2053230X22011335

Meilleur, F. (2023, January). Neutron Scattering in the Biological Sciences: Techniques And Applications. JOVE-JOURNAL OF VISUALIZED EXPERIMENTS, Vol. 1. https://doi.org/10.3791/64806

Dagher, S. F., Vaishnav, A., Stanley, C. B., Meilleur, F., Edwards, B. F. P., & Bruno-Barcena, J. M. (2023). Structural analysis and functional evaluation of the disordered ß-hexosyltransferase region from <i>Hamamotoa (Sporobolomyces) singularis</i>. FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY, 11. https://doi.org/10.3389/fbioe.2023.1291245

Schroder, G. C., William B. O'Dell, Webb, S. P., Agarwal, P. K., & Meilleur, F. (2022, November 2). Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase. CHEMICAL SCIENCE, Vol. 11. https://doi.org/10.1039/D2SC05031E

Tandrup, T., Muderspach, S. J., Banerjee, S., Santoni, G., Ipsen, J. O., Hernandez-Rollan, C., … Lo Leggio, L. (2022). Changes in active-site geometry on X-ray photo-reduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding. IUCRJ, 9(5), 666–681. https://doi.org/10.1107/S2052252522007175

Moreno-Chicano, T., Carey, L. M., Axford, D., Beale, J. H., Doak, R. B., Duyvesteyn, H. M. E., … Hough, M. A. (2022). Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature. IUCRJ, 9, 610–624. https://doi.org/10.1107/S2052252522006418

David, F., Setzler, C., Sorescu, A., Lieberman, R. L., Meilleur, F., & Petty, J. T. (2022, December 1). Mapping H+ in the Nanoscale (A(2)C(4))(2)-Ag-8 Fluorophore. JOURNAL OF PHYSICAL CHEMISTRY LETTERS, Vol. 12. https://doi.org/10.1021/acs.jpclett.2c03161

Dawe, L. N., Manuel Garcia-Ruiz, J., Hadju, J., McIntyre, G. J., Meilleur, F., & Stephenson, L. (2022, April). Teaching and Education highlighted. JOURNAL OF APPLIED CRYSTALLOGRAPHY, Vol. 55, pp. 215–217. https://doi.org/10.1107/S1600576722003661

Sacco, M. D., Hu, Y., Gongora, M. V., Meilleur, F., Kemp, M. T., Zhang, X., … Chen, Y. (2022, March 15). The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition. CELL RESEARCH, Vol. 3. https://doi.org/10.1038/s41422-022-00640-y

Correy, G. J., Kneller, D. W., Phillips, G., Pant, S., Russi, S., Cohen, A. E., … Fraser, J. S. (2022). The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature. SCIENCE ADVANCES, 8(21). https://doi.org/10.1126/sciadv.abo5083

Schröder, G. C., O'Dell, W. B., Webb, S. P., Agarwal, P. K., & Meilleur, F. (2021, December 13). Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase. https://doi.org/10.26434/chemrxiv-2021-n4c1x

Schroeder, G. C., & Meilleur, F. (2021). Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 77(10), 1251–1269. https://doi.org/10.1107/S2059798321009025

Schroder, G. C., William B. O'Dell, Swartz, P. D., & Meilleur, F. (2021). Preliminary results of neutron and X-ray diffraction data collection on a lytic polysaccharide monooxygenase under reduced and acidic conditions. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 77(4), 128–133. https://doi.org/10.1107/S2053230X21002399

Meilleur, F. (2020). A beginner’s guide to neutron macromolecular crystallography. The Biochemist, 42(6), 16–20. https://doi.org/10.1042/BIO20200078

Pierce, J., Cuneo, M. J., Jennings, A., Li, L., Meilleur, F., Zhao, J., & Myles, D. A. A. (2020). Dynamic nuclear polarization enhanced neutron crystallography: Amplifying hydrogen in biological crystals. NEUTRON CRYSTALLOGRAPHY IN STRUCTURAL BIOLOGY, Vol. 634, pp. 153–175. https://doi.org/10.1016/bs.mie.2019.11.018

Meilleur, F., Kovalevsky, A., & Myles, D. A. A. (2020). IMAGINE: The neutron protein crystallography beamline at the high flux isotope reactor. NEUTRON CRYSTALLOGRAPHY IN STRUCTURAL BIOLOGY, Vol. 634, pp. 69–85. https://doi.org/10.1016/bs.mie.2019.11.016

Schroeder, G. C., & Meilleur, F. (2020). Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures. JOVE-JOURNAL OF VISUALIZED EXPERIMENTS, 12(166). https://doi.org/10.3791/61903

Pierce, J., Crow, L., Cuneo, M., Edwards, M., Herwig, K. W., Jennings, A., … Zhao, J. K. (2019). A prototype system for dynamically polarized neutron protein crystallography. NUCLEAR INSTRUMENTS & METHODS IN PHYSICS RESEARCH SECTION A-ACCELERATORS SPECTROMETERS DETECTORS AND ASSOCIATED EQUIPMENT, 940, 430–434. https://doi.org/10.1016/j.nima.2019.06.023

Lu, X., Selvaraj, B., Ghimire-Rijal, S., Orf, G. S., Meilleur, F., Blankenship, R. E., … Myles, D. A. A. (2019). Neutron and X-ray analysis of the Fenna-Matthews-Olson photosynthetic antenna complex from Prosthecochloris aestuarii. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 75(3), 171–175. https://doi.org/10.1107/S2053230X19000724

Knihtila, R., Volmar, A. Y., Meilleur, F., & Mattos, C. (2019). Titration of ionizable groups in proteins using multiple neutron data sets from a single crystal: application to the small GTPase Ras. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 75(2), 111–115. https://doi.org/10.1107/S2053230X18018125

Coates, L., Cao, H. B., Chakoumakos, B. C., Frontzek, M. D., Hoffmann, C., Kovalevsky, A. Y., … Ye, F. (2018). [Review of A suite-level review of the neutron single-crystal diffraction instruments at Oak Ridge National Laboratory]. REVIEW OF SCIENTIFIC INSTRUMENTS, 89(9). https://doi.org/10.1063/1.5030896

Duff, M. R., Jr, Borreguero, J. M., Cuneo, M. J., Ramanathan, A., He, J., Kamath, G., … Agarwal, P. K. (2018). Modulating Enzyme Activity by Altering Protein Dynamics with Solvent. Biochemistry, 57(29), 4263–4275. https://doi.org/10.1021/ACS.BIOCHEM.8B00424

Ashkar, R., Bilheux, H. Z., Bordallo, H., Briber, R., Callaway, D. J. E., Cheng, X., … Smith, J. C. (2018). Neutron scattering in the biological sciences: progress and prospects. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 74, 1129–1168. https://doi.org/10.1107/S2059798318017503

Haberl, B., Dissanayake, S., Wu, Y., Myles, D. A. A., Santos, A. M., Loguillo, M., … Boehler, R. (2018). Next-generation diamond cell and applications to single-crystal neutron diffraction. REVIEW OF SCIENTIFIC INSTRUMENTS, 89(9). https://doi.org/10.1063/1.5031454

Bodenheimer, A. M., ODell, W. B., Oliver, R. C., Qian, S., Stanley, C. B., & Meilleur, F. (2018). Structural investigation of cellobiose dehydrogenase IIA: Insights from small angle scattering into intra- and intermolecular electron transfer mechanisms. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1862(4), 1031–1039. https://doi.org/10.1016/j.bbagen.2018.01.016

Meilleur, F., Coates, L., Cuneo, M. J., Kovalevsky, A., & Myles, D. A. A. (2018). [Review of The Neutron Macromolecular Crystallography Instruments at Oak Ridge National Laboratory: Advances, Challenges, and Opportunities]. CRYSTALS, 8(10). https://doi.org/10.3390/cryst8100388

Golden, E., Yu, L.-J., Meilleur, F., Blakeley, M. P., Duff, A. P., Karton, A., & Vrielink, A. (2017). An extended N-H bond, driven by a conserved second-order interaction, orients the flavin N5 orbital in cholesterol oxidase. Scientific Reports, 7(1), 40517, https://doi.org/10.1038/srep40517

William B. O'Dell, Swartz, P. D., Weiss, K. L., & Meilleur, F. (2017). Crystallization of a fungal lytic polysaccharide monooxygenase expressed from glycoengineered Pichia pastoris for X-ray and neutron diffraction. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 73(2), 70–78. https://doi.org/10.1107/s2053230x16020318

O'Dell, W. B., Agarwal, P. K., & Meilleur, F. (2017). Innentitelbild: Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase (Angew. Chem. 3/2017). Angewandte Chemie. https://doi.org/10.1002/ange.201611987

Li, L., Shukla, S., Meilleur, F., Standaert, R. F., Pierce, J., Myles, D. A. A., & Cuneo, M. J. (2017). Neutron crystallographic studies of T4 lysozyme at cryogenic temperature. PROTEIN SCIENCE, 26(10), 2098–2104. https://doi.org/10.1002/pro.3231

Hiromoto, T., Meilleur, F., Shimizu, R., Shibazaki, C., Adachi, M., Tamada, T., & Kuroki, R. (2017). Neutron structure of the T26H mutant of T4 phage lysozyme provides insight into the catalytic activity of the mutant enzyme and how it differs from that of wild type. PROTEIN SCIENCE, 26(10), 1953–1963. https://doi.org/10.1002/pro.3230

William B. O'Dell, Agarwal, P. K., & Meilleur, F. (2017). Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 56(3), 767–770. https://doi.org/10.1002/anie.201610502

O'Dell, W. B., Agarwal, P. K., & Meilleur, F. (2017). Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase. Angewandte Chemie, 129(3), 785–788. https://doi.org/10.1002/ange.201610502

Bodenheimer, A. M., William B. O'Dell, Stanley, C. B., & Meilleur, F. (2017). Structural studies of Neurospora crassa LPMO9D and redox partner CDHIIA using neutron crystallography and small-angle scattering. CARBOHYDRATE RESEARCH, 448, 200–204. https://doi.org/10.1016/j.carres.2017.03.001

Bodenheimer, A. M., & Meilleur, F. (2016). Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states. FEBS LETTERS, 590(23), 4429–4438. https://doi.org/10.1002/1873-3468.12464

Mascarelli, P. E., Tartara, G. P., Pereyra, N. B., & Maggi, R. G. (2016). Detection of Mycoplasma haemocanis, Mycoplasma haematoparvum, Mycoplasma suis and other vector-borne pathogens in dogs from Córdoba and Santa Fé, Argentina. Parasites & Vectors, 9(1). https://doi.org/10.1186/s13071-016-1920-8

O'Dell, W. B., Agarwal, P. K., & Meilleur, F. (2016). Inside Cover: Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase (Angew. Chem. Int. Ed. 3/2017). Angewandte Chemie International Edition, 56(3), 658–658. https://doi.org/10.1002/anie.201611987

William B. O'Dell, Bodenheimer, A. M., & Meilleur, F. (2016). Neutron protein crystallography: A complementary tool for locating hydrogens in proteins. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 602, 48–60. https://doi.org/10.1016/j.abb.2015.11.033

Zhuravleva, M., Lindsey, A., Chakoumakos, B. C., Custelcean, R., Meilleur, F., Hughes, R. W., … Melcher, C. L. (2015). Crystal structure and thermal expansion of a CsCe2Cl7 scintillator. Journal of Solid State Chemistry, 227, 142–149. https://doi.org/10.1016/J.JSSC.2015.03.032

Knihtila, R., Holzapfel, G., Weiss, K., Meilleur, F., & Mattos, C. (2015). Neutron Crystal Structure of RAS GTPase Puts in Question the Protonation State of the GTP gamma-Phosphate. JOURNAL OF BIOLOGICAL CHEMISTRY, 290(52), 31025–31036. https://doi.org/10.1074/jbc.m115.679860

Golden, E., Attwood, P. V., Duff, A. P., Meilleur, F., & Vrielink, A. (2015). Production and characterization of recombinant perdeuterated cholesterol oxidase. ANALYTICAL BIOCHEMISTRY, 485, 102–108. https://doi.org/10.1016/j.ab.2015.06.008

Bodenheimer, A. M., Cuneo, M. J., Swartz, P. D., He, J., O'Neill, H. M., Myles, D. A., … Section, F. (2014). Crystallization and preliminary X-ray diffraction analysis of Hypocrea jecorina Cel7A in two new crystal forms. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 70(Pt 6), 773–776. https://doi.org/10.1107/s2053230x14008851

Munshi, P., Snell, E. H., Woerd, Mj, J., Ra, M., Da, R., … D. (2014). Neutron structure of the cyclic glucose-bound xylose isomerase E186Q mutant. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 70(Pt 2), 414–420. https://doi.org/10.1107/s1399004713029684

Meilleur, F. (2014). ORNL hosts the participants of the 4thNeutrons in Structural Biology Workshop and the IMAGINE single crystal neutron diffractometer first external users. Neutron News, 25(1), 12–12. https://doi.org/10.1080/10448632.2014.870435

Gruene, T., Hahn, H. W., Luebben, A. V., Meilleur, F., & Sheldrick, G. M. (2014, January). Refinement of macromolecular structures against neutron data with SHELXL2013. JOURNAL OF APPLIED CRYSTALLOGRAPHY, Vol. 47, pp. 462–466. https://doi.org/10.1107/s1600576713027659

Meilleur, F. (2014). The Neutrons in Structural Biology Workshop celebrates its 5th edition. Neutron News, 25(4), 11–11. https://doi.org/10.1080/10448632.2014.955418

Ankner, J. F., Heller, W. T., Herwig, K. W., Meilleur, F., & Myles, D. A. A. (2013, April). Neutron Scattering Techniques and Applications in Structural Biology. Current Protocols in Protein Science. https://doi.org/10.1002/0471140864.ps1716s72

Martin, S. L., He, L., Meilleur, F., Guenther, R. H., Sit, T. L., Lommel, S. A., & Heller, W. T. (2013). New insight into the structure of RNA in red clover necrotic mosaic virus and the role of divalent cations revealed by small-angle neutron scattering. ARCHIVES OF VIROLOGY, 158(8), 1661–1669. https://doi.org/10.1007/s00705-013-1650-6

Meilleur, F., Munshi, P., Robertson, L., Stoica, A. D., Crow, L., Kovalevsky, A., … Acta crystallographica. Section, D. (2013). The IMAGINE instrument: first neutron protein structure and new capabilities for neutron macromolecular crystallography. Biological Crystallography, 69(Pt 10), 2157–2160, https://doi.org/10.1107/s0907444913019604

Meilleur, F. (2013). Third School on the Applications of Neutron Scattering Techniques in Structural Biology, Oak Ridge, TN. Neutron News, 24(1), 4–4. https://doi.org/10.1080/10448632.2013.750140

He, L., Piper, A., Meilleur, F., Hernandez, R., Heller, W. T., & Brown, D. T. (2012). Conformational Changes in Sindbis Virus Induced by Decreased pH Are Revealed by Small-Angle Neutron Scattering. JOURNAL OF VIROLOGY, 86(4), 1982–1987. https://doi.org/10.1128/jvi.06569-11

Myles, D. A. A., Dauvergne, F., Blakeley, M. P., & Meilleur, F. (2012). Neutron protein crystallography at ultra-low (< 15 K) temperatures. JOURNAL OF APPLIED CRYSTALLOGRAPHY, 45(4), 686–692. https://doi.org/10.1107/s0021889812019784

Jayasundar, J. J., Ju, J. H., He, L., Liu, D., Meilleur, F., Zhao, J., … Bu, Z. (2012). Open Conformation of Ezrin Bound to Phosphatidylinositol 4,5-Bisphosphate and to F-actin Revealed by Neutron Scattering. JOURNAL OF BIOLOGICAL CHEMISTRY, 287(44), 37119–37133. https://doi.org/10.1074/jbc.m112.380972

Munshi, P., Chung, S. L., Blakeley, M. P., Weiss, K. L., Myles, D. A., Meilleur, F., & Section, D. (2012). Rapid visualization of hydrogen positions in protein neutron crystallographic structures. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 68(Pt 1), 35–41. https://doi.org/10.1107/s0907444911048402

Pérez, C., Maggi, R. G., Diniz, P. P. V. P., & Breitschwerdt, E. B. (2011). Molecular and Serological Diagnosis of Bartonella Infection in 61 Dogs from the United States. Journal of Veterinary Internal Medicine, 25(4), 805–810. https://doi.org/10.1111/j.1939-1676.2011.0736.x

Borreguero, J. M., He, J., Meilleur, F., Weiss, K. L., Brown, C. M., Myles, D. A., … Agarwal, P. K. (2011). Redox-Promoting Protein Motions in Rubredoxin. JOURNAL OF PHYSICAL CHEMISTRY B, 115(28), 8925–8936. https://doi.org/10.1021/jp201346x

Li, X., Shew, C.-Y., He, L., Meilleur, F., Myles, D. A. A., Liu, E., … Chen, W.-R. (2011). Scattering functions of Platonic solids. JOURNAL OF APPLIED CRYSTALLOGRAPHY, 44, 545–557. https://doi.org/10.1107/s0021889811011691

Martin, S. L., Guenther, R. H., Sit, T. L., Swartz, P. D., Meilleur, F., Lommel, S. A., … Section, F. (2010). Crystallization and preliminary X-ray diffraction analysis of red clover necrotic mosaic virus. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 66(Pt 11), 1458–1462. https://doi.org/10.1107/s1744309110032483

He, L., Piper, A., Meilleur, F., Myles, D. A. A., Hernandez, R., Brown, D. T., & Heller, W. T. (2010). The Structure of Sindbis Virus Produced from Vertebrate and Invertebrate Hosts as Determined by Small-Angle Neutron Scattering. JOURNAL OF VIROLOGY, 84(10), 5270–5276. https://doi.org/10.1128/jvi.00044-10

Gardberg, A. S., Castillo, D., Ar, W., Kl, M., F, B., Mp, M., … D. (2010). Unambiguous determination of H-atom positions: comparing results from neutron and high-resolution X-ray crystallography. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 66(Pt 5), 558–567. https://doi.org/10.1107/s0907444910005494

Meilleur, F., Weiss, K. L., & Myles, D. A. A. (2009). Deuterium Labeling for Neutron Structure-Function-Dynamics Analysis. Micro and Nano Technologies in Bioanalysis, pp. 281–292. https://doi.org/10.1007/978-1-59745-483-4_18

Teixeira, S. C. M., Zaccai, G., Ankner, J., Bellissent-Funel, M. C., Bewley, R., Blakeley, M. P., … Weiss, K. (2008). Erratum to “New sources and instrumentation for neutrons in biology” [Chem. Phys. 345 (2008) 133–151]. Chemical Physics, 351(1-3), 170. https://doi.org/10.1016/j.chemphys.2008.04.007

Teixeira, S. C. M., Zaccai, G., Ankner, J., Bellissent-Funel, M. C., Bewley, R., Blakeley, M. P., … Weiss, K. (2008, April 18). New sources and instrumentation for neutrons in biology. CHEMICAL PHYSICS, Vol. 345, pp. 133–151. https://doi.org/10.1016/j.chemphys.2008.02.030

Teixeira, S. C. M., Zaccai, G., Ankner, J., Bellissent-Funel, M. C., Bewley, R., Blakeley, M. P., … al. (2008). New sources and instrumentation for neutrons in biology (vol 345, pg 133, 2008). Chemical Physics, Vol. 351, pp. 170–170.

Weiss, K. L., Meilleur, F., Blakeley, M. P., Myles, D. A., & Section, F. (2008). Preliminary neutron crystallographic analysis of selectively CH3-protonated deuterated rubredoxin from Pyrococcus furiosus. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 64(Pt 6), 537–540. https://doi.org/10.1107/S1744309108013997

Blakeley, M. P., Ruiz, F., Cachau, R., Hazemann, I., Meilleur, F., Mitschler, A., … Podjarny, A. (2008). Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase. Proceedings of the National Academy of Sciences of the United States of America, 105(6), 1844–1848, https://doi.org/10.1073/pnas.0711659105

Di Costanzo, L., Moulin, M., Haertlein, M., Meilleur, F., & Christianson, D. W. (2007). Expression, purification, assay, and crystal structure of perdeuterated human arginase I. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 465(1), 82–89. https://doi.org/10.1016/j.abb.2007.04.036

Budayova-Spano, M., Bonneté, F., Ferté, N., El Hajji, M., Meilleur, F., Blakeley, M. P., … Acta crystallographica. Section, F. (2006). A preliminary neutron diffraction study of rasburicase, a recombinant urate oxidase enzyme, complexed with 8-azaxanthin. Structural Biology and Crystallization Communications, 62(Pt 3), 306–309, https://doi.org/10.1107/s1744309106006439

Meilleur, F., Snell, E. H., Woerd, M. J., Judge, R. A., & Myles, D. A. A. (2006). A quasi-Laue neutron crystallographic study of d-xylose isomerase. European Biophysics Journal, 35(7), 601–609. https://doi.org/10.1007/s00249-006-0066-6

Blakeley, M. P., Mitschler, A., Hazemann, I., Meilleur, F., Myles, D. A., & Podjarny, A. (2006). Comparison of hydrogen determination with X-ray and neutron crystallography in a human aldose reductase-inhibitor complex. European Biophysics Journal : EBJ, 35(7), 577–583, https://doi.org/10.1007/s00249-006-0064-8

Meilleur, F., Myles, D. A. A., & Blakeley, M. P. (2006). Neutron Laue macromolecular crystallography. European Biophysics Journal, 35(7), 611–620. https://doi.org/10.1007/s00249-006-0074-6

Hazemann, I., Dauvergne, M. T., Blakeley, M. P., Meilleur, F., Haertlein, M., Van Dorsselaer, A., … Acta crystallographica. Section, D. (2005). High-resolution neutron protein crystallography with radically small crystal volumes: application of perdeuteration to human aldose reductase. Biological Crystallography, 61(Pt 10), 1413–1417, https://doi.org/10.1107/s0907444905024285

Bennett, B. C., Meilleur, F., Myles, D. A., Howell, E. E., Dealwis, C. G., Acta crystallographica. Section, D., & crystallography, B. (2005). Preliminary neutron diffraction studies of Escherichia coli dihydrofolate reductase bound to the anticancer drug methotrexate. 61(Pt 5), 574–579, https://doi.org/10.1107/s0907444905004804

Meilleur, F., Dauvergne, M. T., Schlichting, I., Myles, D. A., & Acta crystallographica. Section, D. (2005). Production and X-ray crystallographic analysis of fully deuterated cytochrome P450cam. Biological Crystallography, 61(Pt 5), 539–544, https://doi.org/10.1107/s0907444905003872

Meilleur, F., Contzen, J., Myles, D. A. A., & Jung, C. (2004). Structural Stability and Dynamics of Hydrogenated and Perdeuterated Cytochrome P450cam (CYP101)†. Biochemistry, 43(27), 8744–8753. https://doi.org/10.1021/bi049418q

Adamo, C., Heitzmann, M., Meilleur, F., Rega, N., Scalmani, G., Grand, A., … Barone, V. (2001). Interplay of intrinsic and environmental effects on the magnetic properties of free radicals issuing from H-atom addition to cytosine. Journal of the American Chemical Society, 123(29), 7113–7117, https://doi.org/10.1021/ja004284z