Abstract
Protein crystallographers are nowadays regular users of synchrotron radiation (SR) facilities for several applications. The goal of majority of users is simply to extract more accurate, higher resolution data from existing crystals; they use monochromatic radiation and the rotation method, in order to get a complete survey of the reciprocal space in a short time. In fact the brilliance of SR is essential, due to the weak scattering power of the samples, and because of their sensibility to radiation damage. Over the last few years, however, a general increase of interest for measurements at multiple wavelengths, which exploit the anomalous dispersion for the phase problem (Multiwavelength Anomalous Dispersion - MAD), has generated the need of intense tuneable sources. For these applications, the emphasis is on accurate measurements of the small differences between the intensities of Bragg reflections at various energies across the absorption edge of an element present in the sample. The macromolecular diffraction beamline at ELETTRA, which is now running routinely since spring 1995 has been designed to provide a high flux - highly collimated tuneable X-rays source in the spectral range between 4 and 25 keV. The radiation source is the 57-pole wiggler which delivers a very intense radiation up to 25 keV, and is shared and used simultaneously with the SAXS beamline. The front-end filter system has a cut-off energy at about 4 keV. The beamline optics consists of a pseudo-channel-cut double-crystal monochromator followed by a double focusing toroidal mirror. The tunability and the stability of the monochromator allows the user to perform MAD experiments, and for this purpose, a fluorescence probe for the exact calibration of the absorption edge is available on-line. The experimental station is based on an imaging plate area detector from MarResearch, with a sensible area of 345 mm in diameter. A cooled N2-stream is available to cool the sample crystal in order to reduce the radiation damage. Small Angle X-ray Scattering (SAXS) is an experimental technique used to derive structural information about supra-molecular assemblies, amorphous materials and partly ordered systems (e.g. size and shape of large molecules). The high-flux SAXS beamline at ELETTRA is mainly intended for time-resolved studies on fast structural transitions in the sub-millisecond time region in solutions and in partly ordered systems, triggered by external or process parameters, with a SAXS resolution between 10 and 1400 A in real space. The source is the already mentioned 57-pole and the SAXS beamline accepts 3 discrete energies of its spectrum, namely 5.4, 8 and 16 keV. The beamline optics consists of a flat double-crystal monochromator and a double focusing toroidal mirror. A multi-purpose sample stage, movable along an optical table in order to optimise the sample to detector distance, allows to perform fast time-resolved relaxation studies based on temperature-or pressure-jumps as well as stopped flow experiments. Moreover the users have the possibility to install their own specialised sample surrounding equipment. The optimisation of the beamline with respect to high-flux and consequently high flux density, allows to perform the following experiments: Low Contrast Solution Scattering, Grazing Incidence Surface Diffraction, Micro-Spot Scanning, X-ray Fluorescence Analysis, Time-Resolved Studies ≥11 µs, Simultaneous Small-and Wide- Angle Measurements on Gels, Liquid Crystals, BioPolymers, Amorphous Materials, Muscles
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References
Guinier, A. (1939) Ann. Phys 12 161.
Porod, G. (1951) Kolloid-Z 124 83.
Todd, A.R., Adams, A., Powell, H.R., Wilcock, D.J., Lausi, A., Zanini, F. and Cardin, C.J., Acta Crystallographica D, in press.
Bernstorff, S., Busetto, E., Gramaccioni, C., Lausi, A., Olivi, L., Zanini, F., Savoia, A., Colapietro, M., Portalone, G., Camalli, M., Pifferi, A., Spagna, R., Barba, L. and Cassetta, A. (1995) Rev. Sci. Instrum 66 1661.
Bernstorff, S., Busetto, E., Savoia, A. and Colapietro, M. (1995) Rev. Sci. Instrum 66 2065.
Lausi, A., Gambitta, A. and Bernstorff, S. (1995) Rev. Sci. Instrum 66, 2069.
Fratzl, P., Jakob, H., Rinnerthaler, S., Roschger, P. and Klaushofer, K. (1997) J. Appl. Cryst 30 765.
Zehetbauer, M., Kral, R., Ungar, T., Borbely, A., Ortner, B., Bernstorff, S. and Amenitsch, H. (1996) ELETTRA News 8,http://www.elettra.trieste.it/.
Turkovic, A., Lucic-Lavcevic, M., Drasner, A., Dubcek, P., Milat, O., Etlinger, B., Amenitsch, H. and Rappolt, M. (1998) Materials Science and Engineering B54 174.
Bernstorff, S., Amenitsch, H. and P Laggner, (1998) J. Synch. Radiaton 5 1215.
Amenitsch, H., Bernstorff, S., and Laggner, P. (1995) Rev. Sci. Instrum 66 1624.
Amenitsch, H., Bernstorff, S., Kriechbaum, M., Lombardo, D, Mio, H, Rappolt, M. and Laggner, P. (1997) J. Appl. Cryst 30 872.
Annual Report 1996/1997 of the Austrian SAXS Beamline at ELETTRA, Ch. 2, (1998) Institute for Biophysics and X-ray Structure Research, Austrian Academy of Sciences, Graz, Austria
Rapp, G. and Goody, R.S. (1991) J.Appl.Cryst 24 857.
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Zanini, F., Lausi, A., Savoia, A. (1999). The Beamlines of Elettra and Their Application to Structural Biology. In: Bradbury, E.M., Pongor, S. (eds) Structural Biology and Functional Genomics. NATO Science Series, vol 71. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4631-9_18
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DOI: https://doi.org/10.1007/978-94-011-4631-9_18
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