nach oben

Erschienen in:

2018 | OriginalPaper | Buchkapitel

5. Sample Delivery Techniques for Serial Crystallography

verfasst von : Raymond G. Sierra, Uwe Weierstall, Dominik Oberthuer, Michihiro Sugahara, Eriko Nango, So Iwata, Alke Meents

Erschienen in: X-ray Free Electron Lasers

Verlag: Springer International Publishing

Einloggen

Aktivieren Sie unsere intelligente Suche, um passende Fachinhalte oder Patente zu finden.

search-config

KI-gestützte Suche

Aus

Abstract

In serial femtosecond crystallography (SFX), protein microcrystals and nanocrystals are introduced into the focus of an X-ray free electron laser (FEL) beam ideally one-by-one in a serial fashion. The high photon density in each pulse is the double-edged sword that necessitates the serial nature of the experiments. The high photon count focused spatially and temporally leads to a diffraction-before-destruction snapshot, but this single snapshot is not enough for a high-resolution three-dimensional structural reconstruction. To recover the structure, more snapshots are required to sample all of reciprocal space from randomly oriented crystal diffraction, and in practice, some redundancy is necessary in these measurements. This chapter explores the different sample delivery techniques developed over the years to help enable serial crystallography experiments.

Sie haben noch keine Lizenz? Dann Informieren Sie sich jetzt über unsere Produkte:

Springer Professional "Wirtschaft+Technik"

Online-Abonnement

Mit Springer Professional "Wirtschaft+Technik" erhalten Sie Zugriff auf:

über 102.000 Bücher
über 537 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Finance + Banking
Management + Führung
Marketing + Vertrieb
Maschinenbau + Werkstoffe
Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Springer Professional "Technik"

Online-Abonnement

Mit Springer Professional "Technik" erhalten Sie Zugriff auf:

über 67.000 Bücher
über 390 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Maschinenbau + Werkstoffe

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Vorheriges Kapitel The Lipid Cubic Phase as a Medium for the Growth of Membrane Protein Microcrystals

Nächstes Kapitel When Diffraction Stops and Destruction Begins

Chapman, H. N., Barty, A., Bogan, M. J., Boutet, S., Frank, M., Hau-Riege, S. P., et al. (2006). Femtosecond diffractive imaging with a soft-X-ray free-electron laser. Nature Physics, 2(12), 839–843. https://doi.org/10.1038/nphys461.CrossRef

Stan, C. A., Milathianaki, D., Laksmono, H., Sierra, R. G., McQueen, T. A., Messerschmidt, M., et al. (2016). Liquid explosions induced by X-ray laser pulses. Nature Physics, 12, 966. https://doi.org/10.1038/nphys3779.CrossRef

Chapman, H. N., Fromme, P., Barty, A., White, T. A., Kirian, R. A., Aquila, A., et al. (2011). Femtosecond X-ray protein nanocrystallography. Nature, 470(7332), 73–77. https://doi.org/10.1038/nature09750.CrossRefPubMedPubMedCentral

Seibert, M. M., Ekeberg, T., Maia, F. R. N. C., Svenda, M., Andreasson, J., Jönsson, O., et al. (2011). Single mimivirus particles intercepted and imaged with an X-ray laser. Nature, 470(7332), 78–81. https://doi.org/10.1038/nature09748.CrossRefPubMedPubMedCentral

Bogan, M. J., Benner, W. H., Boutet, S., Rohner, U., Frank, M., Barty, A., et al. (2008). Single particle X-ray diffractive imaging. Nano Letters, 8(1), 310–316. https://doi.org/10.1021/nl072728k.CrossRefPubMed

Awel, S., Kirian, R. A., Wiedorn, M. O., Beyerlein, K. R., Roth, N., Horke, D. A., et al. (2018). Femtosecond X-ray diffraction from an aerosolized beam of protein nanocrystals. Journal of Applied Crystallography, 51(1), 133–139. https://doi.org/10.1107/S1600576717018131.CrossRefPubMedPubMedCentral

Hantke, M. F., Hasse, D., Maia, F. R. N. C., Ekeberg, T., John, K., Svenda, M., et al. (2014). High-throughput imaging of heterogeneous cell organelles with an X-ray laser. Nature Photonics, 8(12), 943–949. https://doi.org/10.1038/nphoton.2014.270.CrossRef

Munke, A., Andreasson, J., Aquila, A., Awel, S., Ayyer, K., Barty, A., et al. (2016). Coherent diffraction of single Rice Dwarf virus particles using hard X-rays at the Linac Coherent Light Source. Scientific Data, 3, 160064. https://doi.org/10.1038/sdata.2016.64.CrossRefPubMedPubMedCentral

Rayleigh, L. (1878). On the instability of jets. Proceedings of the London Mathematical Society, 1(1), 4 Retrieved from http://plms.oxfordjournals.org/content/s1-10/1/4.full.pdf.CrossRef

10.

Rayleigh, L. (1892). XVI. On the instability of a cylinder of viscous liquid under capillary force. The London, Edinburgh, and Dublin Philosophical Magazine and Journal of Science, 34(207), 145–154. https://doi.org/10.1080/14786449208620301.CrossRef

11.

Faubel, M., Schlemmer, S., & Toennies, J. (1988). A molecular beam study of the evaporation of water from a liquid jet. Zeitschrift fur Physik D: Atoms, Molecules and Clusters, 10(2), 269–277 Retrieved from http://www.springerlink.com/index/X6GXW8Q11QV3R085.pdf.CrossRef

12.

Weierstall, U., Doak, R., Spence, J. C. H., Starodub, D., Shapiro, D., Kennedy, P., et al. (2008). Droplet streams for serial crystallography of proteins. Experiments in Fluids, 44(5), 675–689 Retrieved from http://www.springerlink.com/index/Q7N2L3278806078U.pdf.CrossRef

13.

DePonte, D. P., Weierstall, U., Schmidt, K., Warner, J., Starodub, D., Spence, J. C. H., et al. (2008). Gas dynamic virtual nozzle for generation of microscopic droplet streams. Journal of Physics D: Applied Physics, 41(19), 195505. https://doi.org/10.1088/0022-3727/41/19/195505.CrossRef

14.

White, F., & Corfield, I. (2005). Viscous fluid flow (3rd ed.). New York: McGraw-Hill.

15.

Eggers, J., & Villermaux, E. (2008). Physics of liquid jets. Reports on Progress in Physics, 71(1), 1–79. https://doi.org/10.1088/0034-4885/71/3/036601.CrossRef

16.

Gonzalez-Tello, P., Camacho, F., & Blazquez, G. (1994). Density and viscosity of concentrated aqueous solutions of polyethylene glycol. Journal of Chemical & Engineering Data, 39(3), 611–614. https://doi.org/10.1021/je00015a050.CrossRef

17.

Lee, R. J., & Teja, A. S. (1990). Viscosities of poly(ethylene glycols). Journal of Chemical & Engineering Data, 35(4), 385–387. https://doi.org/10.1021/je00062a003.CrossRef

18.

Einstein, A. (1905). On the motion of small particles suspended in a stationary liquid, as required by the molecular kinetic theory of heat. Annalen der Physik, 322, 549–560. https://doi.org/10.1002/andp.19053220806.CrossRef

19.

Probstein, R. F. (1994). Physicochemical hydrodynamics. New York: Wiley. https://doi.org/10.1002/0471725137.CrossRef

20.

Lomb, L., Steinbrener, J., Bari, S., Beisel, D., Berndt, D., Kieser, C., et al. (2012). An anti-settling sample delivery instrument for serial femtosecond crystallography. Journal of Applied Crystallography, 45(4), 1–5. https://doi.org/10.1107/S0021889812024557.CrossRef

21.

Sierra, R. G., Gati, C., Laksmono, H., Dao, E. H., Gul, S., Fuller, F., et al. (2015). Concentric-flow electrokinetic injector enables serial crystallography of ribosome and photosystem II. Nature Methods, 13(1), 59–62. https://doi.org/10.1038/nmeth.3667.CrossRefPubMedPubMedCentral

22.

Johansson, L. C., Arnlund, D., White, T. A., Katona, G., Deponte, D. P., Weierstall, U., et al. (2012). Lipidic phase membrane protein serial femtosecond crystallography. Nature Methods, 9(3), 263–265. https://doi.org/10.1038/nmeth.1867.CrossRefPubMedPubMedCentral

23.

Oberthuer, D., Knoška, J., Wiedorn, M. O., Beyerlein, K. R., Bushnell, D. A., Kovaleva, E. G., et al. (2017). Double-flow focused liquid injector for efficient serial femtosecond crystallography. Scientific Reports, 7, 44628. https://doi.org/10.1038/srep44628.CrossRefPubMedPubMedCentral

24.

Taylor, G. (1953). Dispersion of soluble matter in solvent flowing slowly through a tube. Proceedings of the Royal Society of London A: Mathematical, Physical and Engineering Sciences, 219(1137), 186–203. https://doi.org/10.1098/rspa.1953.0139.CrossRef

25.

Taneda, S. (1979). Visualization of separating Stokes flows. Journal of the Physical Society of Japan, 46(6), 1935–1942. https://doi.org/10.1143/JPSJ.46.1935.CrossRef

26.

Purcell, E. (1976). Life at low Reynolds number. AIP Conference Proceedings, 45, 3–11.

27.

Rayleigh, L. (1879). On the capillary phenomena of jets. Proceedings of the Royal Society of London, 29, 71–97.CrossRef

28.

Frohn, A., & Roth, N. (2000). Dynamics of droplets. Berlin, Germany: Springer Science & Business Media.CrossRef

29.

Gañán-Calvo, A. M. (1998). Generation of steady liquid microthreads and micron-sized monodisperse sprays in gas streams. Physical Review Letters, 80(2), 285.CrossRef

30.

31.

Weierstall, U., Spence, J. C. H., & Doak, R. B. (2012). Injector for scattering measurements on fully solvated biospecies. The Review of Scientific Instruments, 83(3), 035108. CrossRefPubMed

32.

Nelson, G., Kirian, R. A., Weierstall, U., Zatsepin, N. A., Faragó, T., Baumbach, T., et al. (2016). Three-dimensional-printed gas dynamic virtual nozzles for x-ray laser sample delivery. Optics Express, 24(11), 11515–11530.PubMedPubMedCentralCrossRef

33.

Wang, D., Weierstall, U., Pollack, L., & Spence, J. (2014). Double-focusing mixing jet for XFEL study of chemical kinetics. Journal of Synchrotron Radiation, 21(6), 1364–1366.PubMedPubMedCentralCrossRef

34.

Weierstall, U., Doak, R. B., & Spence, J. C. H. (2011). A pump-probe XFEL particle injector for hydrated samples. arXiv preprint arXiv:1105.2104.

35.

Daurer, B. J., Okamoto, K., Bielecki, J., Maia, F. R. N. C., Muhlig, K., Seibert, M. M., et al. (2017). Experimental strategies for imaging bioparticles with femtosecond hard X-ray pulses. IUCrJ, 4(3), 251–262. https://doi.org/10.1107/S2052252517003591.CrossRefPubMedPubMedCentral

36.

Perry, S. L., Guha, S., Pawate, A. S., Bhaskarla, A., Agarwal, V., Nair, S. K., et al. (2013). A microfluidic approach for protein structure determination at room temperature via on-chip anomalous diffraction. Lab on a Chip, 13(16), 3183–3187.PubMedPubMedCentralCrossRef

37.

Zhu, L., Weierstall, U., Cherezov, V., & Liu, W. (2016). Serial femtosecond crystallography of membrane proteins. In I. Moraes (Ed.), The next generation in membrane protein structure determination (pp. 151–160). Cham, Switzerland: Springer.CrossRef

38.

Martin-Garcia, J. M., Conrad, C. E., Nelson, G., Stander, N., Zatsepin, N. A., Zook, J., et al. (2017). Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation. IUCrJ, 4, 439–454. https://doi.org/10.1107/S205225251700570X.CrossRefPubMedPubMedCentral

39.

Tono, K., Nango, E., Sugahara, M., Song, C., Park, J., Tanaka, T., et al. (2015). Diverse application platform for hard X-ray diffraction in SACLA (DAPHNIS): Application to serial protein crystallography using an X-ray free-electron laser. Journal of Synchrotron Radiation, 22, 532–537. https://doi.org/10.1107/S1600577515004464.CrossRefPubMedPubMedCentral

40.

Sugahara, M., Mizohata, E., Nango, E., Suzuki, M., Tanaka, T., Masuda, T., et al. (2015). Grease matrix as a versatile carrier of proteins for serial crystallography. Nature Methods, 12(1), 61–63.CrossRefPubMed

41.

Botha, S., Nass, K., Barends, T. R. M., Kabsch, W., Latz, B., Dworkowski, F., et al. (2015). Room-temperature serial crystallography at synchrotron X-ray sources using slowly flowing free-standing high-viscosity microstreams. Acta Crystallographica. Section D, Biological Crystallography, 71(2), 387.CrossRefPubMed

42.

Conrad, C. E., Basu, S., James, D., Wang, D., Schaffer, A., Roy-Chowdhury, S., et al. (2015). A novel inert crystal delivery medium for serial femtosecond crystallography. IUCrJ, 2(4), 421–430.PubMedPubMedCentralCrossRef

43.

Sugahara, M., Song, C., Suzuki, M., Masuda, T., Inoue, S., Nakane, T., et al. (2016). Oil-free hyaluronic acid matrix for serial femtosecond crystallography. Scientific Reports, 6, 1–6.CrossRef

44.

Kovacsova, G., Grunbein, M. L., Kloos, M., Barends, T. R. M., Schlesinger, R., Heberle, J., et al. (2017). Viscous hydrophilic injection matrices for serial crystallography. IUCrJ, 4, 400–410. https://doi.org/10.1107/S2052252517005140.CrossRefPubMedPubMedCentral

45.

Weierstall, U., James, D., Wang, C., White, T. A., Wang, D., Liu, W., et al. (2014). Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography. Nature Communications, 5, 3309.PubMedCrossRef

46.

Zhang, H., Unal, H., Gati, C., Han, G. W., Liu, W., Zatsepin, N. A., et al. (2015). Structure of the angiotensin receptor revealed by serial femtosecond crystallography. Cell, 161(4), 833–844.PubMedPubMedCentralCrossRef

47.

Fenalti, G., Zatsepin, N. A., Betti, C., Giguere, P., Han, G. W., Ishchenko, A., et al. (2015). Structural basis for bifunctional peptide recognition at human delta-opioid receptor. Nature Structural & Molecular Biology, 22(3), 265–268.CrossRef

48.

Kang, Y., Zhou, X. E., Gao, X., He, Y., Liu, W., Ishchenko, A., et al. (2015). Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature, 523(7562), 561–567.PubMedPubMedCentralCrossRef

49.

Nogly, P., Panneels, V., Nelson, G., Gati, C., Kimura, T., Milne, C., et al. (2016). Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography. Nature Communications, 7, 1–9.CrossRef

50.

Batyuk, A., Galli, L., Ishchenko, A., Han, G. W., Gati, C., Popov, P. A., et al. (2016). Native phasing of x-ray free-electron laser data for a G protein–coupled receptor. Science Advances, 2(9), e1600292.PubMedPubMedCentralCrossRef

51.

Fromme, R., Ishchenko, A., Metz, M., Chowdhury, S. R., Basu, S., Boutet, S., et al. (2015). Serial femtosecond crystallography of soluble proteins in lipidic cubic phase. IUCrJ, 2(5), 545–551.PubMedPubMedCentralCrossRef

52.

James, D., Wang, D., White, T. A., Zatsepin, N., Nelson, G., Liu, H., et al. (2015). Lipidic cubic phase serial millisecond crystallography using synchrotron radiation. IUCrJ, 2(2), 168–176.PubMedPubMedCentralCrossRef

53.

Sierra, R. G., Laksmono, H., Kern, J., Tran, R., Hattne, J., Alonso-Mori, R., et al. (2012). Nanoflow electrospinning serial femtosecond crystallography. Acta Crystallographica. Section D, Biological Crystallography, 68(11), 1584–1587. https://doi.org/10.1107/S0907444912038152.CrossRefPubMedPubMedCentral

54.

Hattne, J., Echols, N., Tran, R., Kern, J., Gildea, R. J., Brewster, A. S., et al. (2014). Accurate macromolecular structures using minimal measurements from X-ray free-electron lasers. Nature Methods, 11(5), 545–548. https://doi.org/10.1038/nmeth.2887.CrossRefPubMedPubMedCentral

55.

Kern, J., Alonso-Mori, R., Hellmich, J., Tran, R., Hattne, J., Laksmono, H., et al. (2012). Room temperature femtosecond X-ray diffraction of photosystem II microcrystals. Proceedings of the National Academy of Sciences of the United States of America, 109(25), 9721–9726. https://doi.org/10.1073/pnas.1204598109.CrossRefPubMedPubMedCentral

56.

Kern, J., Tran, R., Alonso-Mori, R., Koroidov, S., Echols, N., Hattne, J., et al. (2014). Taking snapshots of photosynthetic water oxidation using femtosecond X-ray diffraction and spectroscopy. Nature Communications, 5, 4371. https://doi.org/10.1038/ncomms5371.CrossRefPubMed

57.

Young, I. D., Ibrahim, M., Chatterjee, R., Gul, S., Fuller, F. D., Koroidov, S., et al. (2016). Structure of photosystem II and substrate binding at room temperature. Nature, 540(7633), 453–457. https://doi.org/10.1038/nature20161.CrossRefPubMedPubMedCentral

58.

Alonso-Mori, R., Kern, J., Gildea, R. J., Sokaras, D., Weng, T.-C., Lassalle-Kaiser, B., et al. (2012). Energy-dispersive X-ray emission spectroscopy using an X-ray free-electron laser in a shot-by-shot mode. Proceedings of the National Academy of Sciences of the United States of America, 109(47), 19103. https://doi.org/10.1073/pnas.1211384109.CrossRefPubMedPubMedCentral

59.

Kern, J., Alonso-Mori, R., Tran, R., Hattne, J., Gildea, R. J., Echols, N., et al. (2013). Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem II at room temperature. Science, 340(6131), 491–495. https://doi.org/10.1126/science.1234273.CrossRefPubMedPubMedCentral

60.

Kroll, T., Kern, J., Kubin, M., Ratner, D., Gul, S., Fuller, F. D., et al. (2016). X-ray absorption spectroscopy using a self-seeded soft X-ray free-electron laser. Optics Express, 24(20), 22469. https://doi.org/10.1364/OE.24.022469.CrossRefPubMedPubMedCentral

61.

Kubin, M., Kern, J., Gul, S., Kroll, T., Chatterjee, R., Löchel, H., et al. (2017). Soft x-ray absorption spectroscopy of metalloproteins and high-valent metal-complexes at room temperature using free-electron lasers. Structural Dynamics, 4(5), 054307. https://doi.org/10.1063/1.4986627.CrossRefPubMedPubMedCentral

62.

Mitzner, R., Rehanek, J., Kern, J., Gul, S., Hattne, J., Taguchi, T., et al. (2013). L-edge X-ray absorption spectroscopy of dilute systems relevant to metalloproteins using an X-ray free-electron laser. Journal of Physical Chemistry Letters, 4, 3641–3647. https://doi.org/10.1021/jz401837f.CrossRef

63.

Colletier, J.-P., Sawaya, M. R., Gingery, M., Rodriguez, J. A., Cascio, D., Brewster, A. S., et al. (2016). De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure. Nature, 539(7627), 43–47. https://doi.org/10.1038/nature19825.CrossRefPubMedPubMedCentral

64.

Fernández de la Mora, J. (2007). The fluid dynamics of Taylor cones. Annual Review of Fluid Mechanics, 39(1), 217–243. https://doi.org/10.1146/annurev.fluid.39.050905.110159.CrossRef

65.

Gañán-Calvo, A. M., & Barrero, A. (1999). A novel pneumatic technique to generate steady capillary microjets. Journal of Aerosol Science, 30(1), 117–125. https://doi.org/10.1016/S0021-8502(98)00029-9.CrossRef

66.

Aquila, A., Hunter, M. S., Doak, R. B., Kirian, R. A., Fromme, P., White, T. A., et al. (2012). Time-resolved protein nanocrystallography using an X-ray free-electron laser. Optics Express, 20(3), 2706–2716 Retrieved from http://www.opticsinfobase.org/abstract.cfm?URI=oe-20-3-2706. PubMedPubMedCentralCrossRef

67.

Barty, A., Caleman, C., Aquila, A., Timneanu, N., Lomb, L., White, T. A., et al. (2012). Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements. Nature Photonics, 6(1), 35–40. https://doi.org/10.1038/nphoton.2011.297.CrossRefPubMed

68.

Boutet, S., Lomb, L., Williams, G. J., Barends, T. R. M., Aquila, A., Doak, R. B., et al. (2012). High-resolution protein structure determination by serial femtosecond crystallography. Science, 337(6092), 362–364. https://doi.org/10.1126/science.1217737.CrossRefPubMedPubMedCentral

69.

Koopmann, R., Cupelli, K., Redecke, L., Nass, K., DePonte, D. P., White, T. A., et al. (2012). In vivo protein crystallization opens new routes in structural biology. Nature Methods, 9(3), 259–262. https://doi.org/10.1038/nmeth.1859.CrossRefPubMedPubMedCentral

70.

Lomb, L., Barends, T. R. M., Kassemeyer, S., Aquila, A., Epp, S., Erk, B., et al. (2011). Radiation damage in protein serial femtosecond crystallography using an x-ray free-electron laser. Physical Review B, 84(21), 1–6. https://doi.org/10.1103/PhysRevB.84.214111.CrossRef

71.

Garman, E. (1999). Cool data: Quantity AND quality. Acta Crystallographica, Section D: Biological Crystallography, 55(10), 1641–1653. https://doi.org/10.1107/S0907444999008653.CrossRef

72.

Garman, E. F., & Owen, R. L. (2006). Cryocooling and radiation damage in macromolecular crystallography. Acta Crystallographica, Section D: Biological Crystallography, 62(1), 32–47. https://doi.org/10.1107/S0907444905034207.CrossRef

73.

Ibrahim, M., Chatterjee, R., Hellmich, J., Tran, R., Bommer, M., Yachandra, V. K., et al. (2015). Improvements in serial femtosecond crystallography of photosystem II by optimizing crystal uniformity using microseeding procedures. Structural Dynamics, 2(4), 041705. https://doi.org/10.1063/1.4919741.CrossRefPubMedPubMedCentral

74.

Gañán-Calvo, A. M., & Montanero, J. (2009). Revision of capillary cone-jet physics: Electrospray and flow focusing. Physical Review E, 79(6), 1–18. https://doi.org/10.1103/PhysRevE.79.066305.CrossRef

75.

Liang, M., Williams, G. J., Messerschmidt, M., Seibert, M. M., Montanez, P. A., Hayes, M., et al. (2015). The coherent X-ray imaging instrument at the Linac Coherent Light Source. Journal of Synchrotron Radiation, 22(3), 514–519. https://doi.org/10.1107/S160057751500449X.CrossRefPubMedPubMedCentral

76.

Schlichting, I. (2015). Serial femtosecond crystallography: The first five years. IUCrJ, 2, 246.PubMedPubMedCentralCrossRef

77.

Redecke, L., Nass, K., DePonte, D. P., White, T. A., Rehders, D., Barty, A., et al. (2013). Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser. Science, 339, 227–230.CrossRefPubMed

78.

Emma, P., Akre, R., Arthur, J., Bionta, R., Bostedt, C., Bozek, J., et al. (2010). First lasing and operation of an ångstrom-wavelength free-electron laser. Nature Photonics, 4, 641–647.CrossRef

79.

Beyerlein, K. R., Adriano, L., Heymann, M., Kirian, R., Knoška, J., Wilde, F., et al. (2015). Ceramic micro-injection molded nozzles for serial femtosecond crystallography sample delivery. The Review of Scientific Instruments, 86, 125104.PubMedCrossRef

80.

Barends, T. R., Foucar, L., Ardevol, A., Nass, K., Aquila, A., Botha, S., et al. (2015). Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation. Science, 350, 445–450.CrossRefPubMed

81.

Coquelle, N., Sliwa, M., Woodhouse, J., Schirò, G., Adam, V., Aquila, A., et al. (2018). Chromophore twisting in the excited state of a photoswitchable fluorescent protein captured by time-resolved serial femtosecond crystallography. Nature Chemistry, 10, 31–37.CrossRefPubMed

82.

Pande, K., Hutchison, C. D., Groenhof, G., Aquila, A., Robinson, J. S., Tenboer, J., et al. (2016). Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein. Science, 352, 725–729.PubMedPubMedCentralCrossRef

83.

Tenboer, J., Basu, S., Zatsepin, N., Pande, K., Milathianaki, D., Frank, M., et al. (2014). Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein. Science, 346, 1242–1246.PubMedPubMedCentralCrossRef

84.

Kupitz, C., Olmos Jr., J. L., Holl, M., Tremblay, L., Pande, K., Pandey, S., et al. (2017). Structural enzymology using X-ray free electron lasers. Structural Dynamics, 4(4), 044003.CrossRefPubMed

85.

Stagno, J. R., Liu, Y., Bhandari, Y. R., Conrad, C. E., Panja, S., Swain, M., et al. (2017). Structures of riboswitch RNA reaction states by mix-and-inject XFEL serial crystallography. Nature, 541, 242–246.CrossRefPubMed

86.

Gañán-Calvo, A. M., González-Prieto, R., Riesco-Chueca, P., Herrada, M. A., & Flores-Mosquera, M. (2007). Focusing capillary jets close to the continuum limit. Nature Physics, 3, 737–742.CrossRef

87.

Acero, A. J., Ferrera, C., Montanero, J. M., & Gañán-Calvo, A. M. (2012). Focusing liquid microjets with nozzles. Journal of Micromechanics and Microengineering, 22, 065011.CrossRef

88.

Montanero, J. M., Rebollo-Munoz, N., Herrada, M. A., & Gañán-Calvo, A. M. (2011). Global stability of the focusing effect of fluid jet flows. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics, 83, 036309.PubMedCrossRef

89.

Vega, E. J., Montanero, J. M., Herrada, M. A., & Gañán-Calvo, A. M. (2010). Global and local instability of flow focusing: The influence of the geometry. Physics of Fluids, 22, 064105.CrossRef

90.

Schmidt, M. (2013). Mix and inject: Reaction initiation by diffusion for time-resolved macromolecular crystallography. Advances in Condensed Matter Physics, 2013, 1–10.CrossRef

91.

Calvey, G. D., Katz, A. M., Schaffer, C. B., & Pollack, L. (2016). Mixing injector enables time-resolved crystallography with high hit rate at X-ray free electron lasers. Structural Dynamics, 3, 054301.PubMedPubMedCentralCrossRef

92.

Chavas, L. M., Gumprecht, L., & Chapman, H. N. (2015). Possibilities for serial femtosecond crystallography sample delivery at future light sources. Structural Dynamics, 2, 041709.PubMedPubMedCentralCrossRef

93.

Trebbin, M., Krüger, K., DePonte, D., Roth, S. V., Chapman, H. N., & Förster, S. (2014). Microfluidic liquid jet system with compatibility for atmospheric and high-vacuum conditions. Lab on a Chip, 14, 1733–1745.PubMedCrossRef

94.

Au, A. K., Huynh, W., Horowitz, L. F., & Folch, A. (2016). 3D-printed microfluidics. Angewandte Chemie (International Ed. in English), 55, 3862–3881.CrossRef

95.

Moffat, K. (2014). Time-resolved crystallography and protein design: Signalling photoreceptors and optogenetics. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, 369, 20130568.PubMedPubMedCentralCrossRef

96.

Neutze, R. (2014). Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, 369, 20130318.PubMedPubMedCentralCrossRef

97.

Neutze, R., & Moffat, K. (2012). Time-resolved structural studies at synchrotrons and X-ray free electron lasers: Opportunities and challenges. Current Opinion in Structural Biology, 22, 651–659.PubMedPubMedCentralCrossRef

98.

Schlichting, I., & Goody, R. S. (1997). Triggering methods in crystallographic enzyme kinetics. Methods in Enzymology, 277, 467–490.PubMedCrossRef

99.

Barends, T., White, T. A., Barty, A., Foucar, L., Messerschmidt, M., Alonso-Mori, R., et al. (2015). Effects of self-seeding and crystal post-selection on the quality of Monte Carlo-integrated SFX data. Journal of Synchrotron Radiation, 22, 644.PubMedCrossRef

100.

Brennich, M. E., Nolting, J. F., Dammann, C., Nöding, B., Bauch, S., & Herrmann, H. (2011). Dynamics of intermediate filament assembly followed in micro-flow by small angle X-ray scattering. Lab on a Chip, 11, 708–716.PubMedCrossRef

101.

Knight, J., Vishwanath, A., Brody, J., & Austin, R. (1998). Hydrodynamic focusing on a silicon chip: Mixing nanoliters in microseconds. Physical Review Letters, 80, 3863–3866.CrossRef

102.

Park, H. Y., Qiu, X., Rhoades, E., Korlach, J., Kwok, L. W., & Zipfel, W. R. (2006). Achieving uniform mixing in a microfluidic device: Hydrodynamic focusing prior to mixing. Analytical Chemistry, 78, 4465–4473.PubMedCrossRef

103.

Pollack, L., & Doniach, S. (2009). Time-resolved X-ray scattering and RNA folding. Methods in Enzymology, 469, 253–268.PubMedCrossRef

104.

Pollack, L., Tate, M. W., Darnton, N. C., Knight, J. B., Gruner, S. M., Eaton, W. A., et al. (1999). Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. Proceedings of the National Academy of Sciences, 96, 10115–10117.CrossRef

105.

Zahoor, R., Belšak, G., Bajt, S., Weckert, E., & Hajdu, J. (2018). Simulation of liquid micro-jet in free expanding high-speed co-flowing gas streams. Microfluidics and Nanofluidics, 22, 87. https://doi.org/10.1007/s10404-018-2110-0.CrossRef

106.

Neutze, R., Wouts, R., van der Spoel, D., Weckert, E., & Hajdu, J. (2000). Potential for biomolecular imaging with femtosecond X-ray pulses. Nature, 406, 752–757.PubMedCrossRef

107.

Fukuda, Y., Tse, K. M., Nakane, T., Nakatsu, T., Suzuki, M., Sugahara, M., et al. (2016). Redox-coupled proton transfer mechanism in nitrite reductase revealed by femtosecond crystallography. Proceedings of the National Academy of Sciences of the United States of America, 113, 2928–2933.PubMedPubMedCentralCrossRef

108.

Liu, W., Wacker, D., Gati, C., Han, G. W., James, D., Wang, D., et al. (2013). Serial femtosecond crystallography of G protein–coupled receptors. Science, 342, 1521–1524.PubMedPubMedCentralCrossRef

109.

Mafuné, F., Miyajima, K., Tono, K., Takeda, Y., Kohno, J. Y., Miyauchi, N., et al. (2016). Microcrystal delivery by pulsed liquid droplet for serial femtosecond crystallography. Acta Crystallographica, Section D: Biological Crystallography, 72(Pt 4), 520–523.CrossRef

110.

Zhou, Q., Lai, Y., Bacaj, T., Zhao, M., Lyubimov, A. Y., Uervirojnangkoorn, M., et al. (2015). Architecture of the synaptotagmin–SNARE machinery for neuronal exocytosis. Nature, 525, 62–67.PubMedPubMedCentralCrossRef

111.

Kupitz, C., Basu, S., Grotjohann, I., Fromme, R., Zatsepin, N. A., Rendek, K. N., et al. (2014). Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser. Nature, 513, 261–265.PubMedPubMedCentralCrossRef

112.

Nango, E., Royant, A., Kubo, M., Nakane, T., Wickstrand, C., Kimura, T., et al. (2016). A three dimensional movie of structural changes in bacteriorhodopsin. Science, 354, 1552–1557.CrossRefPubMed

113.

114.

Suga, M., Akita, F., Sugahara, M., Kubo, M., Nakajima, Y., Nakane, T., et al. (2017). Light-induced structural changes and the site of O=O bond formation in PSII caught by XFEL. Nature, 543, 131–135.CrossRefPubMed

115.

Sugahara, M., Song, C., Suzuki, M., Masuda, T., Inoue, S., Nakane, T., et al. (2016). Oil-free hyaluronic acid matrix for serial femtosecond crystallography. Scientific Reports, 6, 24484.PubMedPubMedCentralCrossRef

116.

Sugahara, M., Nakane, T., Masuda, T., Suzuki, M., Inoue, S., Song, C., et al. (2017). Hydroxyethyl cellulose matrix applied to serial crystallography. Scientific Reports, 7, 703.PubMedPubMedCentralCrossRef

117.

Hope, H. (1988). Acta Crystallographica. Section B, 44, 22–26.CrossRef

118.

Nakane, T., Song, C., Suzuki, M., Nango, E., Kobayashi, J., Masuda, T., et al. (2015). Native sulfur/chlorine SAD phasing for serial femtosecond crystallography. Acta Crystallographica Section D: Structural Biology, 71, 2519–2525.CrossRef

119.

Yamashita, K., Pan, D., Okuda, T., Sugahara, M., Kodan, A., Yamaguchi, T., et al. (2015). An isomorphous replacement method for efficient de novo phasing for serial femtosecond crystallography. Scientific Reports, 5, 14017.PubMedPubMedCentralCrossRef

120.

Colletier, J. P., Sliwa, M., Gallat, F. X., Sugahara, M., Guillon, V., Schirò, G., et al. (2016). Serial femtosecond crystallography and ultrafast absorption spectroscopy of the photoswitchable fluorescent protein IrisFP. Journal of Physical Chemistry Letters, 7, 882–887.CrossRef

121.

Nakane, T., Hanashima, S., Suzuki, M., Saiki, H., Hayashi, T., Kakinouchi, K., et al. (2016). Membrane protein structure determination by SAD, SIR or SIRAS phasing in serial femtosecond crystallography using a novel iododetergent. Proceedings of the National Academy of Sciences of the United States of America, 113, 13039–13044.PubMedPubMedCentralCrossRef

122.

Edlund, P., Takala, H., Claesson, E., Henry, L., Dods, R., Lehtivuori, H., et al. (2016). The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography. Scientific Reports, 6, 35279.PubMedPubMedCentralCrossRef

123.

Masuda, T., Suzuki, M., Inoue, S., Song, C., Nakane, T., Nango, E., et al. (2017). Atomic resolution structure of serine protease proteinase K at ambient temperature. Scientific Reports, 7, 45604.PubMedPubMedCentralCrossRef

124.

Cheng, A., Hummel, B., Qiu, H., & Caffrey, M. (1998). A simple mechanical mixer for small viscous lipid-containing samples. Chemistry and Physics of Lipids, 95, 11–21.CrossRefPubMed

125.

Barends, T. R. M., Foucar, L., Botha, S., Doak, R. B., Shoeman, R. L., Nass, K., et al. (2014). De novo protein crystal structure determination from X-ray free-electron laser data. Nature, 505, 244–247.PubMedCrossRef

126.

Hunter, M. S., Yoon, C. H., DeMirci, H., Sierra, R. G., Dao, E. H., Ahmadi, R., et al. (2016). Selenium single-wavelength anomalous diffraction de novo phasing using an X-ray-free electron laser. Nature Communications, 7, 13388.PubMedPubMedCentralCrossRef

127.

Nass, K., Meinhart, A., Barends, T. R., Foucar, L., Gorel, A., Aquila, A., et al. (2016). Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data. IUCrJ, 3, 180–191.PubMedPubMedCentralCrossRef

128.

Thorn, A., & Sheldrick, G. M. (2011). ANODE: Anomalous and heavy-atom density calculation. Journal of Applied Crystallography, 44(6), 1285–1287.PubMedPubMedCentralCrossRef

129.

Stellato, F., Oberthür, D., Liang, M., Bean, R., Gati, C., Yefanov, O., et al. (2014). Room-temperature macromolecular serial crystallography using synchrotron radiation. IUCrJ, 1, 204–212.PubMedPubMedCentralCrossRef

130.

Weierstall, U. (2014). Liquid sample delivery techniques for serial femtosecond crystallography. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, 369, 20130337.PubMedPubMedCentralCrossRef

131.

Nakane, T., Joti, Y., Tono, K., Yabashi, M., Nango, E., Iwata, S., et al. (2016). Data processing pipeline for serial femtosecond crystallography at SACLA. Journal of Applied Crystallography, 49, 1035–1041.PubMedPubMedCentralCrossRef

132.

Roessler, C. G., Agarwal, R., Allaire, M., Alonso-Mori, R., Andi, B., Bachega, J. F. R., et al. (2016). Acoustic injectors for drop-on-demand serial femtosecond crystallography. Structure, 24, 631–640. https://doi.org/10.1016/j.str.2016.02.007.CrossRefPubMedPubMedCentral

133.

Beyerlein, K. R., Dierksmeyer, D., Mariani, V., Kuhn, M., Sarrou, I., Ottaviano, A., et al. (2017). Mix-and-diffuse serial synchrotron crystallography. IUCrJ, 4, 769–777. https://doi.org/10.1107/S2052252517013124.CrossRefPubMedPubMedCentral

134.

Fuller, F. D., Gul, S., Chatterjee, R., Burgie, E. S., Young, I. D., Lebrette, H., et al. (2017). Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers. Nature Methods, 14(4), 443–449.PubMedPubMedCentralCrossRef

135.

Kok, B., Forbush, B., & Mcgloin, M. (1970). Cooperation of charges in photosynthetic O₂ evolution-I. A linear four step mechanism. Photochemistry and Photobiology, 11(6), 457–475. https://doi.org/10.1111/j.1751-1097.1970.tb06017.x.CrossRefPubMed

136.

Hunter, M. S., Segelke, B., Messerschmidt, M., Williams, G. J., Zatsepin, N. A., Barty, A., et al. (2014). Fixed-target protein serial microcrystallography with an x-ray free electron laser. Scientific Reports, 4, 6026.PubMedPubMedCentralCrossRef

137.

Kimura, T., Joti, Y., Shibuya, A., Song, C., Kim, S., Tono, K., et al. (2014). Imaging live cell in micro-liquid enclosure by X-ray laser diffraction. Nature Communications, 5, 3052.PubMedCrossRef

138.

Murray, T. D., Lyubimov, A. Y., Ogata, C. M., Vo, H., Uervirojnangkoorn, M., Brunger, A. T., et al. (2015). A high-transparency, micro-patternable chip for X-ray diffraction analysis of microcrystals under native growth conditions. Acta Crystallographica Section D: Biological Crystallography, 71, 1987–1997.CrossRefPubMedCentral

139.

Cohen, A. E., Soltis, S. M., González, A., Aguila, L., Alonso-Mori, R., Barnes, C. O., et al. (2014). Goniometer-based femtosecond crystallography with X-ray free electron lasers. Proceedings of the National Academy of Sciences of the United States of America, 111, 17122–17127.PubMedPubMedCentralCrossRef

140.

Roedig, P., Vartiainen, I., Duman, R., Panneerselvam, S., Stübe, N., Lorbeer, O., et al. (2015). A micro-patterned silicon chip as sample holder for macromolecular crystallography experiments with minimal background scattering. Scientific Reports, 5, 10451.PubMedPubMedCentralCrossRef

141.

Zarrine-Afsar, A., Barends, T. R. M., Müller, C., Fuchs, M. R., Lomb, L., Schlichting, I., et al. (2012). Crystallography on a chip. Acta Crystallographica Section D: Biological Crystallography, 68, 321–323.CrossRef

142.

Mueller, C., Marx, A., Epp, S. W., Zhong, Y., Kuo, A., Balo, A. R., et al. (2015). Fixed target matrix for femtosecond time-resolved and in situ serial micro-crystallography. Structural Dynamics, 2, 054302. PubMedPubMedCentralCrossRef

143.

Feld, G. K., Heymann, M., Benner, W. H., Pardini, T., Tsai, C. J., Boutet, S., et al. (2015). Low-Z polymer sample supports for fixed-target serial femtosecond X-ray crystallography. Journal of Applied Crystallography, 48(4), 1072–1079.CrossRef

144.

Lyubimov, A. Y., Murray, T. D., Koehl, A., Araci, I. E., Uervirojnangkoorn, M., Zeldin, O. B., et al. (2015). Capture and X-ray diffraction studies of protein microcrystals in a microfluidic trap array. Acta Crystallographica Section D, 71(4), 928–940.CrossRef

145.

Roedig, P., Ginn, H. M., Pakendorf, T., Sutton, G., Harlos, K., Walter, T. S., et al. (2017). High-speed fixed-target serial virus crystallography. Nature Methods, 14, 805. https://doi.org/10.1038/nmeth.4335.CrossRefPubMedPubMedCentral

146.

Opara, N., Martiel, I., Arnold, S. A., Braun, T., Stahlberg, H., Makita, M., et al. (2017). Direct protein crystallization on ultrathin membranes for diffraction measurements at X-ray free-electron lasers. Journal of Applied Crystallography, 50, 909–918.CrossRef

147.

Meents, A., Gutmann, S., Wagner, A., & Schulze-Briese, C. (2009). Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures. Proceedings of the National Academy of Sciences, 107(3), 1094–1099. https://doi.org/10.1073/pnas.0905481107.CrossRef

148.

Owen, R. L., Rudiño-Piñera, E., & Garman, E. F. (2006). Experimental determination of the radiation dose limit for cryocooled protein crystals. Proc Natl Acad Sci USA, 103(13), 4912–4917.PubMedCrossRefPubMedCentral

149.

Suga, M., Akita, F., Hirata, K., Ueno, G., Murakami, H., Nakajima, Y., et al. (2015). Native structure of photosystem II at 1.95 Å resolution viewed by femtosecond X-ray pulses. Nature, 517(7532), 99–103. https://doi.org/10.1038/nature13991.CrossRefPubMed

150.

Fraser, J. S., van den Bedemb, H., Samelsona, A. J., Langa, P. T., Holton, J. M., et al. (2011). Proceedings of the National Academy of Sciences of the United States of America, 108(39), 16247–16252. https://doi.org/10.1073/pnas.1111325108.CrossRefPubMedPubMedCentral

151.

Coquelle, N., Brewster, A. S., Kapp, U., Shilova, A., Weinhausen, B., Burghammer, M., et al. (2015). Raster-scanning serial protein crystallography using micro- and nano-focused synchrotron beams. Acta Crystallographica Section D: Biological Crystallography, 71(Pt 5), 1184–1196. https://doi.org/10.1107/S1399004715004514 Epub 2015 Apr 25.CrossRefPubMedCentral

152.

Sui, S., Wang, Y., Kolewe, K. W., Srajer, V., Henning, R., Schiffman, J. D., et al. (2016). Graphene-based microfluidics for serial crystallography. Lab on a Chip, 16(16), 3082–3096. https://doi.org/10.1039/c6lc00451b.CrossRefPubMedPubMedCentral

153.

Kiefersauer, R., Than, M. E., Dobbek, H., Gremer, L., Melero, M., Strobl, S., et al. (2000). Journal of Applied Crystallography, 33, 1223–1230.CrossRef

154.

Sanchez Weatherby, J., Bowler, M. W., Huet, J., Gobbo, A., Felisaz, F., Lavault, B., et al. (2009). Improving diffraction by humidity control: A novel device compatible with X-ray beamlines. Acta Crystallographica. Section D, Biological Crystallography, 65, 1237–1246.PubMedCrossRef

155.

Roedig, P., Duman, R., Sanchez-Weatherby, J., Vartiainen, I., Burkhardt, A., Warmer, M., et al. (2016). Room-temperature macromolecular crystallography using a micro-patterned silicon chip with minimal background scattering. Journal of Applied Crystallography, 49, 968–975.PubMedPubMedCentralCrossRef

156.

Meents, A., Wiedorn, M. O., Srajer, V., Henning, R., Sarrou, I., Bergtholdt, J., et al. (2017). Pink beam serial crystallography. Nature Communications, 8, 1281. https://doi.org/10.1038/s41467-017-01417-3.CrossRefPubMedPubMedCentral

157.

Sherrell, D. A., Foster, A. J., Hudson, L., Nutter, B., O’Hea, J., Nelson, S., et al. (2015). A modular and compact portable mini-endstation for high-precision, high-speed fixed target serial crystallography at FEL and synchrotron sources. Journal of Synchrotron Radiation, 22, 1372–1378.PubMedPubMedCentralCrossRef

158.

Owen, R. L., Axford, D., Sherrell, D. A., Kuo, A., Ernst, O. P., Schulz, E. C., et al. (2017). Low-dose fixed-target serial synchrotron crystallography. Acta Crystallographica Section D: Biological Crystallography, 73, 373–378.CrossRef

159.

Abdallah, B. G., Zatsepin, N. a., Roy-Chowdhury, S., Coe, J., Conrad, C. E., Dörner, K., et al. (2015). Microfluidic sorting of protein nanocrystals by size for X-ray free-electron laser diffraction. Structural Dynamics, 2, 041719. https://doi.org/10.1063/1.4928688.CrossRefPubMedPubMedCentral

160.

Koralek, J. D., Kim, J. B., Brůža, P., Curry, C. B., Chen, Z., Bechtel, H. A., et al. (2018). Generation and characterization of ultrathin free-flowing liquid sheets. Nature Communications, 9(1), 1–8. https://doi.org/10.1038/s41467-018-03696-w.CrossRef

161.

Wiedorn, M. O., Awel, S., Morgan, A. J., Ayyer, K., Gevorkov, Y., Fleckenstein, H., et al. (2018). Rapid sample delivery for megahertz serial crystallography at X-ray FELs. IUCrJ, 5(5), 574–584.PubMedPubMedCentralCrossRef

Titel: Sample Delivery Techniques for Serial Crystallography
verfasst von: Raymond G. Sierra
Uwe Weierstall
Dominik Oberthuer
Michihiro Sugahara
Eriko Nango
So Iwata
Alke Meents
Verlag: Springer International Publishing
Buch: X-ray Free Electron Lasers
Print ISBN: 978-3-030-00550-4

Electronic ISBN: 978-3-030-00551-1

Copyright-Jahr: 2018
DOI: https://doi.org/10.1007/978-3-030-00551-1_5

Neuer Inhalt

Bildnachweise

VDI-Icon, Profil Icon, inhalt2, Springer Professional Modul/© Springer Fachmedien Wiesbaden GmbH, Nachhaltigkeitsaward Key Visual/© Cometis AG/Global ESG Monitor | Daniel Rupp | Generiert mit KI, Search Icon, Banner Hanser, Arbeitszeit/© granata68 / Fotolia, E-Autos im Fuhrpark: Lohnt sich das noch?/© Petair / stock.adobe.com, Kryptowährungen/© gopixa / Getty Images / iStock, Zeitschrift Wissensmanagement Cover, PatentFit-Logo/© Springer Fachmedien Wiesbaden GmbH, Sustainibility Finance/© Robert Kneschke / stock.adobe.com / Springer Fachmedien Wiesbaden GmbH, Zukunftswerkstatt Sales Excellence 2024/© AndreyPopov / Getty Images / iStock, 2023_Antrieb/© supervisuell

Springer Professional

Abstract

Bitte loggen Sie sich ein, um Zugang zu Ihrer Lizenz zu erhalten.

Sie haben noch keine Lizenz? Dann Informieren Sie sich jetzt über unsere Produkte:

Springer Professional "Wirtschaft+Technik"

Springer Professional "Technik"

Neuer Inhalt

Bitte loggen Sie sich ein, um Zugang zu Ihrer Lizenz zu erhalten.

Bitte loggen Sie sich ein, um Zugang zu Ihrer Lizenz zu erhalten.