Flora Meilleur

Tel : + 1 865 576 5230

Fax : + 1 865 574 8363

e-mail: meilleurf@ornl.gov


Assistant Professor

PhD in Biophysics, X-ray and neutron crystallographic analysis of cytochrome P450cam and D-xylose isomerase.International PhD program of the European Molecular Biology Laboratory (EMBL)and Université Joseph Fourier, Grenoble (France) 

Diplômes d'Etude Approfondie (DEA) (master’s degree) in NMR andcrystallography for biology, Université Joseph Fourier, Grenoble (France)

Research training: EMBL & Commissariat à l'Energie Atomique, Grenoble (France) Neutron crystallographic analysis and quantum chemistry study of myoglobin

Maîtrise in Chemistry and Physics, Université Joseph Fourier, Grenoble (France)

Research training: Commissariat à l'Energie Atomique, Grenoble (France).Quantum chemistry study of H-atom addition to cytosine

  
   
       

RESEARCH INTERESTS 

            Our  research is in the biophysical chemistry of proteins, focusing on structure and function relationships. We are using a combination of high resolution X-ray crystallography and neutron crystallography. While X-ray crystallography is the most powerful diffraction technique that can be used to determine the 3D structures of biomolecules at atomic resolution, neutron crystallography provides a powerful and unique complement to X-ray analysis enabling key and individual hydrogen atoms to be located that cannot be seen by X-ray analysis alone.

            Hydrogen atoms (~50% of the total atoms in biomolecules) are often the workhorses of bio-chemical reactions. While the absence of information on hydrogen location do not hamper accurate determination of 3D structures, visualization of hydrogen becomes critical when the purpose of the analysis is to understand how biomolecules carry out chemical reactions.

Detailed Research Interests: Dr. Flora Meilleur

SELECTED PUBLICATIONS

[1]. Meilleur F., Myles D.A., Blakeley M.P. (2006) Eur. Biophys. J ., 611-620. Neutron Laue macromolecular crystallography.

[2]. Meilleur F., Snell E.H., van der Woerd M.J., Judge R.A., Myles D.A. (2006) Eur. Biophys. J., 601-609. A Quasi-Laue Neutron Crystallographic Study of D-Xylose Isomerase.

[3]. Snell E.H., van der Woerd M.J, Damon M., Judge R.A., Myles D.A., Meilleur F. (2006) Eur. Biophys. J., 621-632. Optimizing crystal volume for neutron diffraction: Xylose Isomerase

[4]. Budayova-Spano M., Bonnete F., Ferte N., El Hajji M., Meilleur F., Blakeley M.P., Castro B. (2006) Acta Cryst., F62: 306-309.A preliminary neutron diffraction study of rasburicase, a recombinant urate oxidase enzyme, complexed with 8-azaxanthin.

[5]. Bennett B.C., Meilleur F., Myles D.A., Howell E.E., Dealwis C.G. (2005) Acta Cryst. D61, 574-579. Preliminary neutron diffraction studies of Escherichia coli dihydrofolate reductase bound to the anticancer drug methotrexate

[6]. Meilleur F., Dauvergne M.T., Schlichting I., Myles D.A.A*. (2005) Acta Cryst. D61, 539-544. X-Ray crystallographic analysis of fully deuterated cytochrome P450cam

[7]. Meilleur F., Contzen J., Myles D.A.A., Jung C. (2004) Biochemistry. 43, 8744-8753. Structural stability and dynamics of hydrogenated and perdeuterated cytochrome P450cam (CYP101).

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