Scientist

 


ESRF
71 Avenue des Martyrs
CS 40220
38043 Grenoble Cedex 9 - France
Tel : +33 (0)47688 2938
email : vonstett-at-esrf.fr

 

 

List of publications

  1. G. Gotthard, D. von Stetten, D. Clavel, M. Noirclerc-Savoye, and A. Royant, Chromophore isomer stabilization is critical to efficient fluorescence in Cyan Fluorescent Proteins, Biochemistry , in press (2017).
  2. D. von Stetten, T. Giraud, S. Bui, R.A. Steiner, F. Fihman, D. de Sanctis, and A. Royant, Online Raman spectroscopy for structural biology on beamline ID29 of the ESRF, J. Struct. Biol. 200, 124-127 (2017).
  3. J. Kalms, A. Schmidt, S. Frielingsdorf, P. van der Linden, D. von Stetten, O. Lenz, P. Carpentier, and P. Scheerer, Krypton derivatization of an O2-tolerant membrane-bound [NiFe] hydrogenase reveals a hydrophobic tunnel network for gas transport, Angew. Chem. Int. Ed. 55, 5586-5590 (2016).
  4. D. Clavel, G. Gotthard, D. von Stetten, D. de Sanctis, H. Pasquier, G.G. Lambert, N.C. Shaner, and A. Royant, Structural analysis of the bright monomeric yellow-green fluorescent protein mNeonGreen obtained by directed evolution, Acta Cryst. D72, 1298-1307 (2016).
  5. M.W. Bowler, D. Nurizzo, R. Barrett, A. Beteva, M. Bodin, H. Caserotto, S. Delageniere, F. Dobias, D. Flot, T. Giraud, N. Guichard, M. Guijarro, M. Lentini, G.A. Leonard, S. McSweeney, M. Oskarsson, W. Schmidt, A. Snigirev, D. von Stetten, J. Surr, O. Svensson, P. Theveneau, and C. Mueller-Dieckmann, MASSIF-1: a beamline dedicated to the fully automatic characterization and data collection from crystals of biological macromolecules, J. Synchrotron Rad. 22, 1540-1547 (2015).   Open Access!
  6. F. Velazquez Escobar, D. von Stetten, M. Günther-Lütkens, A. Keidel, N. Michael, T. Lamparter, L.-O. Essen, J. Hughes, W. Gärtner, Y. Yang, K. Heyne, M.A. Mroginski, and P. Hildebrandt, Conformational heterogeneity of the Pfr chromophore in plant and cyanobacterial phytochromes, Front. Mol. Biosci. 2:37 (2015).   Open Access!
  7. P. Scheerer, F. Zhang, J. Kalms, D. von Stetten, N. Krauß, I. Oberpichler, and T. Lamparter, The class III cyclobutane pyrimidine dimer photolyase structure reveals a new antenna chromophore binding site and alternative photoreduction pathways, J. Biol. Chem. 290, 11504-11514 (2015).
  8. C. Mueller-Dieckmann, M.W. Bowler, P. Carpentier, D. Flot, A.A. McCarthy, M.H. Nanao, D. Nurizzo, P. Pernot, A. Popov, A. Round, A. Royant, D. de Sanctis, D. von Stetten, and G.A. Leonard, The status of the macromolecular crystallography beamlines at the European Synchrotron Radiation Facility, Eur. Phys. J. Plus 130:70 (2015).
  9. D. von Stetten, T. Giraud, P. Carpentier, F. Sever, M. Terrien, F. Dobias, D.H. Juers, D. Flot, C. Mueller-Dieckmann, G.A. Leonard, D. de Sanctis, and A. Royant, In crystallo optical spectroscopy (icOS) as a complementary tool on the macromolecular crystallography beamlines of the ESRF, Acta Cryst. D71, 15-26 (2015).   Open Access!
  10. S. Bui, D. von Stetten, P.G. Jambrina, T. Prangé, N. Colloc'h, D. de Sanctis, A. Royant, E. Rosta, and R.A. Steiner, Direct evidence for a peroxide intermediate and a reactive enzyme–substrate–dioxygen configuration in a cofactor-free oxidase, Angew. Chem. 126, 13930–13934 (2014).   Open Access!
  11. M. Szczepek, F. Beyrière, K.P. Hofmann, M. Elgeti, R. Kazmin, A. Rose, F.J. Bartl, D. von Stetten, M. Heck, M.E. Sommer, P.W. Hildebrand, and P. Scheerer, Crystal structure of a common GPCR-binding interface for G protein and arrestin, Nature Commun. 5, 4801 (2014).   Open Access!
  12. V. Polovinkin, T. Balandin, O. Volkov, E. Round, V. Borshchevskiy, P. Utrobin, D. von Stetten, A. Royant, D. Willbold, G. Arzumanyan, V. Chupin, J.L. Popot, and V. Gordeliy, Nanoparticle surface-enhanced Raman scattering of bacteriorhodopsin stabilized by amphipol A8-35, J. Membrane Biol. 247 , 971-980 (2014).
  13. F. Bonnot, E. Tremey, D. von Stetten, S. Rat, S. Duval, P. Carpentier, M. Clemancey, A. Desbois, and V. Nivière, Formation of high-valent iron-oxo species in superoxide reductase: characterization by resonance Raman spectroscopy, Angew. Chem. Int. Ed. 53, 5926-5930 (2014).
  14. K. Anders, G. Daminelli-Widany, M.A. Mroginski, D. von Stetten, and L.-O. Essen, Structure of the cyanobacterial phytochrome 2 photosensor implies a tryptophan switch for phytochrome signaling, J. Biol. Chem. 288, 35714-35725 (2013).   Open Access!
  15. J. Salewski, F. Velazquez Escobar, S. Kaminski, D. von Stetten, A. Keidel, Y. Rippers, N. Michael, P. Scheerer, P. Piwowarski, F. Bartl, N. Frankenberg-Dinkel, S. Ringsdorf, W. Gaertner, T. Lamparter, M.A. Mroginski, and P. Hildebrandt, The structure of the biliverdin cofactor in the Pfr state of bathy and prototypical phytochromes, J. Biol. Chem. 288, 16800-16814 (2013).   Open Access!
  16. W.Y. Wahlgren, H. Omran, D. von Stetten, A. Royant, S. van der Post, and G. Katona, Structural characterization of bacterioferritin from Blastochloris viridis, PLoS ONE 7, e46992 (2012).   Open Access!
  17. D. von Stetten, G. Batot, M. Noirclerc-Savoye, and A. Royant, Alteration of fluorescent protein spectroscopic properties upon cryoprotection, Acta Cryst. D68, 1578-1583 (2012).
  18. D. von Stetten, M. Noirclerc-Savoye, J. Goedhart, T.W.J. Gadella, and A. Royant, Structure of a fluorescent protein from Aequorea victoria bearing the obligate-monomer mutation A206K, Acta Cryst. F68, 878-882 (2012).
  19. J. Goedhart*, D. von Stetten*, M. Noirclerc-Savoye, M. Lelimousin, L. Joosen, M.A. Hink, L. van Weeren, T.W.J. Gadella Jr., and Antoine Royant, Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%, Nature Commun. 3, 751 (2012).   Open Access!
  20. M.A. Mroginski, D. von Stetten, S. Kaminski, F. Velazquez Escobar, N. Michael, G. Daminelli-Widany, and P. Hildebrandt, Elucidating photoinduced structural changes in phytochromes by the combined application of resonance Raman spectroscopy and theoretical methods, J. Molec. Struct. 993, 15-25 (2011).
  21. M.A. Mroginski, S. Kaminski, D. von Stetten, S. Ringsdorf, W. Gärtner, L.-O. Essen, and P. Hildebrandt, Structure of the chromophore binding pocket in the Pr state of plant phytochrome phyA, J. Phys. Chem. B 115, 1220-1231 (2011).
  22. K. Anders, D. von Stetten, J. Mailliet, S. Kiontke, V.A. Sineshchekov, P. Hildebrandt, J. Hughes, and L.-O. Essen, Spectroscopic and photochemical characterization of the red-light sensitive photosensory module of Cph2 from Synechocystis PCC 6803, Photochem. Photobiol. 87, 160-173 (2011).
  23. A. Keidel, D. von Stetten, C. Rodrigues, C. Maguas, and P. Hildebrandt, Discrimination of green Arabica and Robusta coffee beans by Raman spectroscopy, J. Agric. Food Chem. 58, 11187-11192 (2010).
  24. P. Piwowarski, E. Ritter, K.-P. Hofmann, P. Hildebrandt, D. von Stetten, P. Scheerer, N. Michael, T. Lamparter, and F. Bartl, Light-induced activation of bacterial phytochrome Agp1 monitored by static and time-resolved FTIR spectroscopy, ChemPhysChem 11, 1207-1214 (2010).
  25. S. Kaminski, M. Gaus, P. Phatak, D. von Stetten, M. Elstner, and M.A. Mroginski, Vibrational Raman spectra from the self-consistent charge density functional tight binding method via classical time-correlation functions, J. Chem. Theory Comput. 6, 1240-1255 (2010).
  26. A.T. Ulijasz, G. Cornilescu, D. von Stetten, C. Cornilescu, F. Velazquez Escobar, J. Zhang, R.J. Stankey, M. Rivera, P. Hildebrandt, and R.D. Vierstra, Cyanochromes are blue/green photoreversible photoreceptors defined by a stable double cysteine linkage to a phycoviolobilin-type chromophore, J. Biol. Chem. 284, 29757-29772 (2009).   Open Access!
    (Note also the cover of that issue.)
  27. M.-A. Mroginski, D. von Stetten, F. Velazquez Escobar, H.M. Strauss, S. Kaminski, P. Scheerer, M. Günther, D.H. Murgida, P. Schmieder, C. Bongards, W. Gärtner, J. Mailliet, J. Hughes, L.-O. Essen, and P. Hildebrandt, Chromophore structure of cyanobacterial phytochrome Cph1 in the Pr state: reconciling structural and spectroscopic data by QM/MM calculations, Biophys. J. 96, 4153-4163 (2009).   Open Access!
  28. S. Brandt, D. von Stetten, M. Günther, P. Hildebrandt, and N. Frankenberg-Dinkel, The fungal phytochrome FphA from Aspergillus nidulans, J. Biol. Chem. 283, 34605-34614 (2008).   Open Access!
  29. A. T. Ulijasz, G. Cornilescu, D. von Stetten, S. Kaminski, M.A. Mroginski,J. Zhang, D. Bhaya, P. Hildebrandt, and R.D. Vierstra, Characterization of two thermostable cyanobacterial phytochromes reveals global movements in the chromophore-binding domain during photoconversion, J. Biol. Chem. 283, 21251-21266 (2008).   Open Access!
  30. D. von Stetten, M. Günther, P. Scheerer, D.H. Murgida, M.A. Mroginski, N. Krauß, T. Lamparter, J. Zhang, D.M. Anstrom, R.D. Vierstra, K.T. Forest, and P. Hildebrandt, Chromophore heterogeneity and photoconversion in phytochrome crystals and solutions studied by Resonance Raman spectroscopy, Angew. Chem. Int. Ed. 47, 4753-4755 (2008); Resonanz-Raman-spektroskopische Untersuchung der Chromophorheterogenität und Photokonversion in Phytochromkristallen und -lösungen, Angew. Chem. 120, 4831-4833 (2008).
  31. J.R. Wagner, J. Zhang, D. von Stetten, M. Günther, D.H. Murgida, M.A. Mroginski, J.M. Walker, K.T. Forest, P. Hildebrandt, and R.D. Vierstra, Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes, J. Biol. Chem. 283, 12212-12226 (2008).   Open Access!
  32. D. von Stetten, S. Seibeck, N. Michael, P. Scheerer, M.A. Mroginski, D.H. Murgida, N. Krauss, M.P. Heyn, P. Hildebrandt, B. Borucki, and T. Lamparter, Highly conserved residues Asp-197 and His-250 in Agp1 phytochrome control the proton affinity of the chromophore and Pfr formation, J. Biol. Chem. 282, 2116-2123 (2007).   Open Access!
  33. D.H. Murgida, D. von Stetten, P. Hildebrandt, P. Schwinte, F. Siebert, S. Sharda, W. Gärtner, and M.A. Mroginski, The chromophore structures of the Pr states in plant and bacterial phytochromes, Biophys. J. 93, 2410-2417 (2007).   Open Access!
  34. B. Borucki, D. von Stetten, S. Seibeck, T. Lamparter, N. Michael, M.A. Mroginski, H. Otto, D.H. Murgida, M.P. Heyn, and P. Hildebrandt, Light-induced proton release of phytochrome is coupled to the transient deprotonation of the tetrapyrrole chromophore, J. Biol. Chem. 280, 34358-34364 (2005).   Open Access!
  35. M.A. Mroginski, D.H. Murgida, D. von Stetten, C. Kneip, F. Mark, and P. Hildebrandt, Determination of the chromophore structures in the photoinduced reaction cycle of phytochrome, J. Amer. Chem. Soc. 126, 16734-16735 (2004).