Abstract
In spite of the recent advances in the X-Ray crystallography and nuclear magnetic resonance techniques, the determination of the quaternary structure of large protein complexes is still a challenge in molecular biology and biological sciences. In this respect, small-angle X-ray scattering (SAXS) is a key technique, enabling the determination of the possible structural conformation of complexes in an almost native state. Despite of this book being devoted to scattering techniques by synchrotron radiation, in this chapter we present two examples of application of laboratory-based SAXS to protein solution. The fundaments of the technique are obviously the same and have been deeply described in Chap. 2. In this chapter, we will introduce the application of SAXS to protein solution. Special emphasis is done on data reduction and absolute units calibration. As an example to illustrate the power of this technique, two new data sets for two protein complexes will be presented. This will show how high-quality SAXS data combined with advanced model strategies enables the determination of the quaternary structure of protein complexes.
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Oliveira, C., Vorup-Jensen, T., Andersen, C., Andersen, G., Pedersen, J. (2009). Discovering New Features of Protein Complexes Structures by Small-Angle X-Ray Scattering. In: Gomez, M., Nogales, A., Garcia-Gutierrez, M., Ezquerra, T. (eds) Applications of Synchrotron Light to Scattering and Diffraction in Materials and Life Sciences. Lecture Notes in Physics, vol 776. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-95968-7_11
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DOI: https://doi.org/10.1007/978-3-540-95968-7_11
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