Faculty Assistant

Maura E. Matvey
Frick Laboratory, 121

Research Focus

Nozomi Ando video interviewWhat are the structural dynamics involved in protein allostery and catalysis? How do flexible enzymes perform challenging chemistry? Can we animate crystal structures of proteins? These are outstanding questions in biology, which motivate studies of proteins in motion.

Capturing molecular movies of proteins in action is the next frontier of structural enzymology. Towards this goal, our group will develop advanced X-ray based methods, such as time-resolved X-ray scattering, in order to examine the role of structural dynamics in enzyme function at multiple length- and timescales. Enzymes that utilize metal-containing cofactors (i.e. metalloenzymes) are of particular interest to our research, both for the fascinating reactions that they are able to catalyze and for their physical properties. In addition to performing biochemical and biophysical characterizations in-house, our group will design and fabricate devices and heavily utilize synchrotron X-rays.

Research Areas
Chemical Biology
Spectroscopy / Physical Chemistry

NIH Pathway to Independence Award (2012-2014)

NIH Ruth L. Kirschstein National Research Service Award (2010-2011)

Invited plenary speaker, 15th International Small Angle Scattering Conference (2012)

Cornell High Energy Synchrotron Source Executive User Committee, elected (2011-2013)

Selected Recent Publications

Skou, S.; Gillilan, R. E.; Ando, N., "Synchrotron-based small-angle X-ray scattering of proteins in solution." Nature Protocols 2014, 9 (7), 1727-1739.

Minnihan, E. C.; Ando, N.; Brignole, E. J.; Olshansky, L.; Chittuluru, J.; Asturias, F. J.; Drennan, C. L.; Nocera, D. G.; Stubbe, J., "Generation of a stable, aminotyrosyl radical-induced alpha 2 beta 2 complex of Escherichia coli class Ia ribonucleotide reductase." Proceedings of the National Academy of Sciences of the United States of America 2013, 110 (10), 3835-3840.

​Kung, Y.; Ando, N.; Doukov, T. I.; Blasiak, L. C.; Bender, G.; Seravalli, J.; Ragsdale, S. W.; Drennan, C. L., "Visualizing molecular juggling within a B-12-dependent methyltransferase complex." Nature 2012, 484 (7393), 265-U159.

Ando, N.; Kung, Y.; Can, M.; Bender, G.; Ragsdale, S. W.; Drennan, C. L., "Transient B-12-Dependent Methyltransferase Complexes Revealed by Small-Angle X-ray Scattering." Journal of the American Chemical Society 2012, 134 (43), 17945-17954.

Wang, S.; Meng, Y.-f.; Ando, N.; Tate, M.; Krasnicki, S.; Yan, C.-s.; Liang, Q.; Lai, J.; Mao, H.-k.; Gruner, S. M.; Hemley, R. J., "Single-crystal CVD diamonds as small-angle X-ray scattering windows for high-pressure research." Journal of Applied Crystallography 2012, 45, 453-457.

Bewley, K. D.; Firer-Sherwood, M. A.; Mock, J.-Y.; Ando, N.; Drennan, C. L.; Elliott, S. J., "Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family." Biochemical Society Transactions 2012, 40, 1268-U144.

Brignole, E. J.; Ando, N.; Zimanyi, C. M.; Drennan, C. L., "The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years." Biochemical Society Transactions 2012, 40, 523-530.

Zimanyi, C. M.; Ando, N.; Brignole, E. J.; Asturias, F. J.; Stubbe, J.; Drennan, C. L., "Tangled Up in Knots: Structures of Inactivated Forms of E. coli Class Ia Ribonucleotide Reductase." Structure 2012, 20 (8), 1374-1383.

Firer-Sherwood, M. A.; Ando, N.; Drennan, C. L.; Elliott, S. J., "Solution-Based Structural Analysis of the Decaheme Cytochrome, MtrA, by Small-Angle X-ray Scattering and Analytical Ultracentrifugation." Journal of Physical Chemistry B 2011, 115 (38), 11208-11214.

Ando, N.; Brignole, E. J.; Zimanyi, C. M.; Funk, M. A.; Yokoyama, K.; Asturias, F. J.; Stubbe, J.; Drennan, C. L., "Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase." Proceedings of the National Academy of Sciences of the United States of America 2011, 108 (52), 21046-21051.

Barstow, B.; Ando, N.; Kim, C. U.; Gruner, S. M., "Coupling of Pressure-Induced Structural Shifts to Spectral Changes in a Yellow Fluorescent Protein." Biophysical Journal 2009, 97 (6), 1719-1727.

Barstow, B.; Ando, N.; Kim, C. U.; Gruner, S. M., "Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift." Proceedings of the National Academy of Sciences of the United States of America 2008, 105 (36), 13362-13366.

Gotoh, T.; Ando, N.; Kikuchi, K.-I., "Analysis of inactivation of AcMNPV under various conditions by the ELVA method. "Bioscience Biotechnology and Biochemistry 2008, 72 (7), 1973-1976.

Ando, N.; Barstow, B.; Baase, W. A.; Fields, A.; Matthews, B. W.; Gruner, S. M., "Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation." Biochemistry 2008, 47 (42), 11097-11109.

Ando, N.; Chenevier, P.; Novak, M.; Tate, M. W.; Gruner, S. M., "High hydrostatic pressure small-angle X-ray scattering cell for protein solution studies featuring diamond windows and disposable sample cells." Journal of Applied Crystallography 2008, 41, 167-175.

Polozova, A.; Li, X. G.; Shangguan, T.; Meers, P.; Schuette, D. R.; Ando, N.; Gruner, S. M.; Perkins, W. R., "Formation of homogeneous unilamellar liposomes from an interdigitated matrix." Biochimica Et Biophysica Acta-Biomembranes 2005, 1668 (1), 117-125.