Publications

Articles in peer-reviewed journals

[2000] [2001] [2002] [2003] [2004] [2005] [2006] [2007] [2008] [2009] [2010] [2011] [2012] [2013] [2014] [2015] [2016] [2017] [2018] [2019] [2020] [2021]

Crystallogenesis studies on yeast aspartyl-tRNA synthetase. Use of phase diagram to improve crystal quality. C. Sauter, B. Lorber, D. Kern, J. Cavarelli, D. Moras & R. Giegé Acta Cryst. D (1999), 55: 149-156 [PDF] Copyright © International Union of Crystallography.

Effect of additives on the crystallization of proteins and nucleic acids. C. Sauter, J.D. Ng, B. Lorber, G. Keith, P. Brion, D.W. Hosseini, J.M. Lehn & R. Giegé. J. Crystal Growth (1999), 196: 365-376 [PDF].

Characterization of protein and virus crystals by quasi-planar wave topography: A comparison between crystals grown in solution and in agarose gel. B. Lorber, C. Sauter, J.D. Ng, D.W. Zhu, R. Giegé, O. Vidal, M.C. Robert & B. Capelle. J. Crystal Growth (1999), 204: 357-368 [PDF].

Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals. B. Lorber, C. Sauter, M.C. Robert, B. Capelle & R. Giegé. Acta Cryst. D (1999), 55: 1491-1494 [PDF] Copyright © International Union of Crystallography.

A sulfate pocket formed by three GU pairs in the 0.97 Å resolution X-ray structure of a nonameric RNA. B. Masquida, C. Sauter & E. Westhof. RNA (1999), 5: 1384-1395 [PDF].

Mimics of yeast tRNAAsp and their recognition by aspartyl-tRNA synthetase. A. Wolfson, A. Khvorova, C. Sauter, C. Florentz & R. Giegé. Biochemistry (1999), 38:11926-11932 [PDF].

The free aspartyl-tRNA synthetase differs from the tRNA-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon binding domain. C. Sauter, B. Lorber, J. Cavarelli, D. Moras & R. Giegé. J. Mol. Biol (2000), 299: 1333-1344 [PDF].

Protein crystallization: A history of a supersaturation wave. J.M. García-Ruiz, F. Otólora, M.L. Novella, J.A. Gavira, C. Sauter & O. Vidal. J. Crystal Growth (2001), 232: 149-155. [PDF].

Crystallogenesis in tRNA aminoacylation systems: how packing accounts for crystallization drawbacks with yeast aspartyl-tRNA synthetase. C. Sauter, B. Lorber, A. Théobald-Dietrich & R. Giegé. J. Crystal Growth (2001), 232: 399-408. [PDF].

Packing contacts in orthorhombic and monoclinic crystals of a thermophilic aspartyl-tRNA synthetase favor the hydrophobic regions of the protein. D.W. Zhu, J.D. Ng, D. Kern, B. Lorber & R. Giegé. J. Crystal Growth (2001), 232: 376-386. [PDF].

Growth kinetics, diffraction properties and effect of agarose on the stability of a novel crystal form of  T. thermophilus aspartyl-tRNA synthetase-1. D.W. Zhu, B. Lorber, C. Sauter, J.D. Ng, P. Bénas, C. Le Grimellec & R. Giegé. Acta Cryst. D 2001), 57: 552-558. [PDF] Copyright © International Union of Crystallography.

Structure of Tetragonal Hen Egg White Lysozyme at 0.94 Å from Crystals Grown by the Counter-Diffusion Method. C. Sauter, F. Otálora, J.A. Gavira, O. Vidal, R. Giegé & J.M. García-Ruiz. Acta Cryst. D (2001), 57: 1119-1126. [PDF] Copyright © International Union of Crystallography.

Towards atomic resolution with crystals grown in gel: The case of thaumatin seen at room temperature. C. Sauter, B. Lorber & R. Giegé. Proteins: Struc. Func. Genet. (2002), 48: 146-150. [PDF] Copyright © Wiley.

Comparative analysis of space- and earth-grown crystals of an aminoacyl-tRNA synthetase: Space crystals are more useful for structure determination. J.D. Ng, C. Sauter, B. Lorber, N. Kirkland, J. Arnez & R. Giegé. Acta Cryst. D (2002), 58: 645-652. [PDF] Copyright © International Union of Crystallography.

Crystallization of biological macromolecules using agarose gel. C. Biertümpfel, J. Basquin, D. Suck & C. Sauter. Acta Cryst. D (2002), 58: 1657-1659. [PDF] Copyright © International Union of Crystallography.

From conventional crystallization to better crystals from space: a review on pilot crystallogenesis studies with aspartyl-tRNA synthetases. B. Lorber, A. Théobald-Dietrich, C. Charron, C. Sauter, J.D. Ng, D.W. Zhu & R. Giegé. Acta Cryst. D (2002), 58: 1674-1680. [PDF] Copyright © International Union of Crystallography.

Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. Common features of RNA binding in Archaea and Eucarya. S. Thore, C. Mayer, C. Sauter, S. Weeks & D. Suck. J. Biol. Chem. (2003), 278: 1239-1247. [PDF]

Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli. C. Sauter, J. Basquin & D. Suck. Nucleic Acid Res. (2003), 31: 4194-4198. [PDF]

Crystallization and preliminary X-ray characterization of the atypical glutaminyl-tRNA synthetase from Deinococcus radiodurans. M.A. Deniziak, C. Sauter, H.D. Becker, R. Giegé & D. Kern. Acta Cryst. D (2004) 60: 2361-2363. [PDF] Copyright © International Union of Crystallography.

Effects of macromolecular impurities and of crystallization method on the quality of eubacterial aspartyl-tRNA synthetase crystals. A. Moreno, A. Théobald-Dietrich, B. Lorber, C. Sauter & R. Giegé. Acta Cryst. D (2005) 61: 789-792. [PDF] Copyright © International Union of Crystallography.

Characterization of crystals of the Hjc resolvase from Archaeoglobus fulgidus grown in gel by counter-diffusion. C. Biertümpfel, J.Basquin, D. Suck & C. Sauter. Acta Cryst. F (2005), 61: 684-687. [PDF] Copyright © International Union of Crystallography.

Lessons from crystals grown in the Advanced Protein Crystallisation Facility for conventional crystallisation applied to structural biology. A. Vergara, B. Lorber, C. Sauter, R. Giegé & A. Zagari. Biophysical Chemistry (2005), 118: 102-112. [PDF]

Loss of a Primordial Identity Element for a Mammalian Mitochondrial Aminoacylation System. A. Fender, C. Sauter, M. Messmer, Joern Pútz, R. Giegé, C. Florentz & M. Sissler. J. Biol. Chem. (2006), 281: 15980 - 15986. [PDF]

Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation. M. Deniziak, C. Sauter, H.D. Becker, C.A. Paulus, R. Giegé & D. Kern. Nucleic Acids Res. (2007), 35: 1421-31.[PDF] [PDF(small)]

Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial amino-acyl-tRNA synthetase. L. Bonnefond, M. Frugier, E. Touzé, B. Lorber, C. Florentz, R. Giegé, J. Rudinger-Thirion & C. Sauter. Acta Cryst. F (2007), 63: 338-341. [PDF]

Disorder can exist inside well-diffracting crystals. E. Touzé, B. Lorber, M.A. Deniziak, H.D. Becker, D. Kern., R. Giegé & C. Sauter. Crystal Growth & Design (2007), 7: 2195-2197. [PDF]

human mitochondrial TyrRS space Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features. L. Bonnefond, M. Frugier, E. Touzé, B. Lorber, C. Florentz, R. Giegé, C. Sauter & J. Rudinger-Thirion. Structure (2007), 15: 1505-1516. [PDF] [Supplement]

From Macrofluidics to microfluidics for the crystallization of biological macromolecules. C. Sauter, K. Dhouib & B. Lorber. Crystal Growth & Design (2007), 7: 2247-2250. [PDF]

Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon. M. Blaise, V. Olieric, C. Sauter, B. Lorber, B. Roy, S. Karmakar, R. Banerjee, H.D. Becker, D. Kern. J. Mol. Biol. (2008) 381, 1224-37. [PDF]

Crystallogenesis trends of free and liganded aminoacyl-tRNA synthetases. R. Giegé, E. Touzé, A. Théobald-Dietrich, B. Lorber & C. Sauter. Crystal Growth & Design (2008), 8: 4297-306. [PDF]

Agarose gel facilitates enzyme crystal soaking with a ligand analog. C. Sauter, C. Balg, A. Moreno, K. Dhouib, A. Théobald-Dietrich, R. Chêvert, R. Giegé & B. Lorber. J. Applied Crystallography (2009), 42: 279-283. [PDF] Copyright © International Union of Crystallography.

Microfluidic chips for the crystallization of biomacromolecules by counter-diffusion and on-chip crystal X-ray analysis. K. Dhouib, C. Khan Malek, W. Pfleging, B. Gauthier-Manuel, R. Duffait, G. Thuillier, R. Ferrigno, L. Jacquamet, J. Ohana, J.L. Ferrer, A. Théobald-Dietrich, R. Giegé &, B. Lorber C. Sauter. Lab-on-a-Chip (2009), 9: 1412 - 1421. [PDF]

Peculiar Inhibition of Human Mitochondrial Aspartyl-tRNA Synthetase by Adenylate Analogs. M. Messmer, S.P. Blais, C. Balg, R. Chênevert, L. Grenier, P. Lagüe, C. Sauter, M. Sissler, R. Giegé, J. Lapointe & C. Florentz. Biochimie (2009), 91: 596-603. [PDF]

Tertiary network in mammalian mitochondrial tRNAAsp revealed by solution probing and phylogeny. M. Messmer, J. Pütz, T. Suzuki, T. Suzuki, C. Sauter, M. Sissler & C. Florentz. Nucleic Acids Res. (2009), 37: 6881-6895. [PDF]

Crystal growth of proteins, nucleic acids, and viruses in gels. B. Lorber, C. Sauter, A. Théobald-Dietrich, A. Moreno, P. Schellenberger, M.-C. Robert, B. Capelle, S. Sanglier, N. Potier & R. Giegé. Prog. Biophys. Mol. Biol. (2009), 101: 13-25. [PDF]

Biocrystallography: past, present, future. R. Giegé & C. Sauter. HFSP journal (Frontiers in Life Science) (2010), 4: 109-121. [PDF]

Strategies for the Crystallization of Viruses: Using phase diagrams and gels to produce 3D crystals of Grapevine fanleaf virus. P. Schellenberger, G. Demangeat, O. Lemaire, C. Ritzenthaler, M. Bergdoll, V. Oliéric, C. Sauter & B. Lorber. J. Structural Biology (2011), 174: 344-351. [PDF]

Structural insights into viral determinants of nematode mediated Grapevine fanleaf virus transmission. P. Schellenberger, C. Sauter, B. Lorber, P. Bron, S. Trapani, M. Bergdoll, A. Marmonier, C. Schmitt-Keichinger, O. Lemaire, G. Demangeat & C. Ritzenthaler. PLOS Pathogens (2011), 7: e1002034. [PDF]

Crystal Structure of the Archaeal Asparagine Synthetase: Interrelation with Aspartyl-tRNA and Asparaginyl-tRNA Synthetases. M. Blaise, M. Fréchin, V. Oliéric, C. Charron, C. Sauter, B. Lorber, H. Roy & D. Kern.. J. Mol. Biol. (2011), 412: 437-452. [PDF]

Exploiting protein engineering and crystal polymorphism for successful X-ray structure determination. L. Bonnefond, P. Schellenberger, J. Basquin, G. Demangeat, C. Ritzenthaler, R. Chênevert, C. Balg, M. Frugier, J. Rudinger-Thirion, R. Giegé, B. Lorber & C. Sauter. Crystal Growth & Design. (2011), 11: 4334-4343. [PDF] (ACS Articles on Request)

Structure of transfer RNAs: similarity and variability. R. Giegé, F. Jühling, J. Pütz, P. Stadler P, C. Sauter & C. Florentz. WIREs RNA (2012), 3:37-61. [PDF]

Predicting protein crystallizability and nucleation. N. Sanchez-Puig, C. Sauter, B. Lorber, R. Giegé & A. Moreno. Protein and peptide letters (2012), 19:725-731. [PDF]

Re-designed N-terminus enhances expression, solubility and crystallizability of mitochondrial protein. A. Gaudry, B. Lorber, A. Neuenfeldt, C. Sauter, C. Florentz & M. Sissler. Protein engineering, design & selection (2012), 25:473-481. [PDF]

Structural insights into protein-only RNase P complexed with tRNA. A. Gobert, F. Pinker, O. Fuchsbauer, B. Gutmann, R. Boutin, P. Roblin, C. Sauter & P. Giegé. Nature communications (2013), 4:1353. [PDF][Supp]

Thermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture. A. Neuenfeldt, B. Lorber, E. Ennifar, A. Gaudry, C. Sauter, M. Sissler & C. Florentz. Nucleic Acids Res. (2013), 41: 2698-2708. [PDF][Supp]

PPR proteins shed a new light on RNase P biology. F. Pinker, G. Bonnard, A. Gobert, O. Fuchsbauer, B. Gutmann, K. Hammani, C. Sauter, P.A. Gegenheimer & P. Giegé. RNA biology (2013), 10: 1457–1468. [PDF]

ChipX: a novel microfluidic chip for counter-diffusion crystallization of biomolecules and in situ crystal analysis at room temperature. F. Pinker, M. Brun, P. Morin, A.-L. Deman, J.-F. Chateaux, V. Oliéric, C. Stirnimann, B. Lorber, N. Terrier, Nicolas, R. Ferrigno & C. Sauter. Crystal Growth & Design (2013), 13: 3333–3340. [PDF]

Crystal structure of 3WJ core revealing divalent ion-promoted thermostability and assembly of the Phi29 hexameric motor pRNA. H. Zhang, J.A. Endrizzi, Y. Shu, F. Haque, C. Sauter, L.S. Shlyakhtenko, Y. Lyubchenko, P. Guo & Y.I. Chi. RNA (2013), 19: 1226-1237. [PDF]

Molecular basis for the differential interaction of plant mitochondrial VDAC proteins with tRNAs. T. Salinas, S. El Farouk-Ameqrane, E. Ubrig, C. Sauter, A.-M. Duchêne & L. Maréchal-Drouard. Nucleic Acids Res. (2014), 42: 9937-9948. [PDF] [Supp]

Crystallization and crystallographic analysis of an Arabidopsis nuclear proteinaceous RNase P. F. Pinker, P. Giegé & C. Sauter. Acta Crystallographica Section F: Structural Biology Communications (2015), F71:1372-77. [PDF]

Neurodegenerative disease-associated mutants of a human mitochondrial aminoacyl-tRNA synthetase present individual molecular signatures. C. Sauter, B. Lorber, A. Gaudry, L. Karim, H. Schwenzer, F. Wien, P. Roblin, C. Florentz & M. Sissler. Scientific Reports (2015), 5: 17332. [PDF] [Supp]

Transfer RNA: from pioneering crystallographic studies to contemporary tRNA biology. P. Fernández-Millán, C. Schelcher, J. Chihade, B. Masquida, P. Giegé & C. Sauter. Archives of Biochemistry and Biophysics (2016), 602: 95-105. [PDF]

Mechanistic and structural studies of Protein-Only RNase P compared to ribonucleoproteins reveal the two faces of the same enzymatic activity. C. Schelcher, C. Sauter & P. Giegé. Biomolecules (2016), 6: E30. [PDF]

Display of whole proteins on inner and outer surfaces of grapevine fanleaf virus-like particles. L. Belval, C. Hemmer, C. Sauter, J.D. Fauny, F. Berthold, L. Ackerer, C. Schmitt-Keichinger, O. Lemaire, G. Demangeat & C. Ritzenthaler. Plant Biotechnol J. (2016), 14: 2288-2299. [PDF]

PRORP : tRNA complex space Biophysical analysis of Arabidopsis protein-only RNase P alone and in complex with tRNA provides a refined model of tRNA binding. F. Pinker, C. Schelcher, P. Fernández-Millán, A. Gobert, P. Roblin, A. Thureau, C. Birck, P. Giegé & C. Sauter. J. Biol. Chem. (2017), 292: 13904-13913. [PDF]

armless tRNA space Small but large enough: structural properties of armless mitochondrial tRNAs from the nematode Romanomermis culicivorax. T. Jühling, E. Duchardt-Ferner, S. Bonin, J. Wöhnert, J. Pütz, C. Florentz, H. Betat, C. Sauter & M. Mörl. Nucleic Acids Res. (2018), 46: 9170-9180. [PDF] [Supp]

Combining crystallogenesis methods to produce diffraction quality crystals of a psychrophilic tRNA maturating enzyme. R. de Wijn, O. Hennig, B. Lorber, F. Ernst, H. Betat, M. Mörl & C. Sauter. Acta Crystallographica Section F: Structural Biology Communications (2018), 74: 747-753. [PDF]

A simple and versatile microfluidic device for efficient biomacromolecule crystallization and structural analysis by serial crystallography. R. de Wijn, O. Hennig, J. Roche, S. Engilberge, K. Rollet, P. Fernandez-Millan, K. Brillet, H. Betat, M. Mörl, A. Roussel, E. Girard, C. Mueller-Dieckmann, G.C. Fox, V. Oliéric, J.A. Gavira, B. Lorber & C. Sauter. IUCrJ (2019), 6: 454–464. [PDF] [Supp]

XtalController study space Monitoring the production of high diffraction-quality crystals of two enzymes in real time using in situ dynamic light scattering. R. de Wijn, K. Rollet, S. Engilberge, A.G. McEwen, O. Hennig, H. Betat, M. Mörl, F. Riobé, O. Maury, E. Girard, P. Bénas, B. Lorber & C. Sauter. Crystals (2020), 10: 65-77. [PDF], [BioRxiv]

Structural basis of nanobody-recognition of grapevine fanleaf virus and of virus resistance loss. I. Orlov, C. Hemmer, L. Ackerer, B. Lorber, A. Ghannam, V. Poignavent, K. Hleibieh, C. Sauter, C. Schmitt-Keichinger, L. Belval, J.M. Hily, A. Marmonier, V. Komar, S. Gersch, P. Schellenberger, P. Bron, E. Vigne, S. Muyldermans, O. Lemaire, G. Demangeat, C. Ritzenthaler & B.P. Klaholz. PNAS (2020), 117: 10848-10855. [html], [BioRxiv]

Adaptation of the Romanomermis culicivorax CCA-adding enzyme to miniaturized armless tRNA substrates. O. Hennig, S. Philipp, S. Bonin, K. Rollet, T. Kolberg, T. Jühling, H. Betat, C. Sauter & M. Mörl. International Journal of Molecular Sciences (2020), in press. [PDF]

Crystallization and structure determination of an enzyme:substrate complex by serial crystallography in a versatile microfluidic chip. R. de Wijn, K. Rollet, V. Olieric, O. Hennig, N. Thome, C. Nous, C. Paulus, B. Lorber, H. Betat, M. Mörl & C. Sauter. Journal of Visualized Experiments (2021), in press. [VIDEO]

Book chapters [Top]

La cristallogenèse des macromolécules biologiques. R. Giegé, C. Sauter, D.W. Zhu, J.D. Ng & B. Lorber. In Images de la Recherche en Biologie Structurale. Presses du CNRS, Paris (2000), 145-151. [Abstract] [Full text].

Crystallization -- General Methods (ch. 4.1). C. Sauter, B. Lorber, A. McPherson & R. Giegé. In International Tables of Crystallography, Vol. F, Crystallography of Biological Macromolecules (2nd edition), edited by E. Arnold, D.M. Himmel & M.G. Rossmann, Chichester: John Wiley and Sons (2012), 99-120. [HTML] [PDF]

Translation in mammalian mitochondria : Order and disorder linked to tRNAs and aminoacyl-tRNA synthetases. C. Florentz, J. Pütz, F. Jühling, H. Schwenzer, P. Stadler, B. Lorber, C. Sauter & M. Sissler. In Translation in Mitochondria and Other Organelles, edited by A.M. Duchêne, Springer Verlag (2013), 55-83.

Crystallization of RNA. G. Kondo, C. Sauter & B. Masquida. In Handbook of RNA biochemistry (2nd edition), edited by R.K. Hartmann, A. Bindereif, A. Schön, E. Westhof, Weinhiem, Wiley-VCH Verlag GmbH & Co. (2014), 481-498.

Structural Analysis of RNA by Small-Angle X-ray Scattering. A. Théobald-Dietrich, R. de Wijn, K. Rollet, A. Bluhm, J. Rudinger-Thirion, C. Paulus, B. Lorber, A. Thureau, M. Frugier & C. Sauter in RNA spectroscopy: Methods and Protocols, Methods in Molecular Biology, edited by V. Arluison & F. Wien, New-York, Springer Science+Business Media (2020), 189-215. [PDF].

Patent [Top]

Dispositif microfluidique pour la cristallisation et l'analyse cristallographique de molécules. C. Sauter, B. Lorber, A. Théobald-Dietrich, R. Giegé, C. Khan-Malek, B. Gauthier-Manuel, G. Thuillier, R. Ferrigno. French Patent (19/07/2006), FR 06/06583.

Other publications [Top]

Compte rendu " 7th International Conference on the Crystallization of Biological Macromolecules". C. Sauter. Regard sur la Biochimie (1998), 4: 66-68.

Cristallogenèse de macromolécules biologiques en vue d'études structurales: Application à des molécules modèles et aux composants de systèmes d'aminoacylation des ARNt. C. Sauter. Ph.D. Thesis, Université Louis Pasteur, Strasbourg, 8 June 1999.

Results of four experiments in the Advanced Protein Crystallization Facility (APCF): Improved protein crystal growth in space. B. Lorber, C. Sauter & R. Giegé. LowG Journal (1999), 3: 4-7 [PDF].

Characterization of protein crystals grown in microgravity during STS-95 missions: Comparison of high resolution data sets of thaumatin crystals in gel on earth or in space. B. Lorber, C. Sauter, J.D. Ng & R. Giegé. Annual report 1998, M. Wilmanns & V. Lamzin, ed., EMBL Outstation at DESY, Hamburg (1999), 321-322.

La cristallogenèse des macromolécules biologiques. C. Sauter & R. Giegé. In Regard sur la Biochimie (2001), 3:21-31. [PDF].

Crystal growth in microgravity can yield better protein structures: The examples of thaumatin and aspartyl-tRNA synthetase. A.Théobald-Dietrich, B. Lorber, J.D Ng, C. Sauter, C. Charron, M.-C. Robert, B. Capelle & R. Giegé. Proceedings of the First International Symposium on Microgravity Research and Applications in Physical Sciences and Biotechnology (2001), 457-463.

Structural basis of protein-nucleic acid interactions. Group of D. Suck. EMBL research reports (2002), 171-175. [PDF]

Compte rendu "10th International Conference on the Crystallization of Biological Macromolecules". C. Sauter. Regard sur la Biochimie (2005), 1: 46-47. [PDF]

Compte rendu "11th International Conference on the Crystallization of Biological Macromolecules". E. Touzé & C. Sauter. Regard sur la Biochimie (2006), 11: 8.

Cristallogenèse biologiques : aspects fondamentaux et appliqués. C. Sauter. Habilitation à Diriger des Recherches, Université Louis Pasteur, Strasbourg, 26 octobre 2007.

The novel RNase P in action. A. Gobert, F. Pinker, O. Fuchsbauer, B. Gutmann, B. Boutin, P. Roblin, C. Sauter & P. Giegé. Synchrotron highlights 2013, Synchrotron SOLEIL, Saint-Aubin, (2014) 64-65. [PDF]

armless tRNA space Les ARN manchots d’animaux sans patte. C. Sauter. En direct des labos, Site INSB-CNRS, 15 octobre 2018. [HTML]

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