Abstract
Small-angle scattering, solution scattering from proteins in solution, reflects the shape of the scatter as a spread of electron density, which is common to protein crystallography. Although the obtained resolution of small-angle scattering is inferior to that of crystallography, it shows the global image of protein structure in solution without constraints of neighboring molecules in crystal lattice. At ambient pressure, data collection technology and analyses of small-angle scattering method developed so greatly in recent 10 years that it is recognized as one of the powerful method of structural biology. In parallel, many efforts have been made to apply this technique under high pressure. The instrumentation and interpretation of small-angle scattering under pressure, however, requires special considerations. The present chapter reviews the technological aspect of scattering from protein solution especially optimized for synchrotron X-ray sources.
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Acknowledgements
The author thanks to Drs. Masato Moritoki and Hiroshi Matsuo for their help in designing HP-cells. Drs. Ryo Ishiguro and Takaaki Hikima and Mr. Ryosuke Noda contributed to the data collection of nitrilase. All HP-SAXS experiments were done at BL45XU-SAXS, SPring-8, Harima with the approval of RIKEN (Proposal Nos. 20080035, 20100104, 20110050, 20120089, 20130092).
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Fujisawa, T. (2015). High Pressure Small-Angle X-Ray Scattering. In: Akasaka, K., Matsuki, H. (eds) High Pressure Bioscience. Subcellular Biochemistry, vol 72. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-9918-8_30
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DOI: https://doi.org/10.1007/978-94-017-9918-8_30
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