International
Tables for
Crystallography
Volume H
Powder diffraction
Edited by C. J. Gilmore, J. A. Kaduk and H. Schenk

International Tables for Crystallography (2018). Vol. H, ch. 2.7, p. 161

Section 2.7.6. Soft and biomaterials under pressure

A. Katrusiaka*

aFaculty of Chemistry, Adam Mickiewicz University, Poznań, Poland
Correspondence e-mail: katran@amu.edu.pl

2.7.6. Soft and biomaterials under pressure

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Interest in the effects of pressure on biological materials is connected to the processing of food and the search for methods of modifying the structure of living tissue and its functions. Soft biological compounds, including proteins, membranes, surfactants, lipids, polymer mesophases and other macromolecular assemblies present in living tissue, are susceptible to pressure, which can affect the molecular conformation and arrangement with relatively low energies of transformation (Royer, 2002[link]). Medium pressure suffices for protein coagulation, as observed for egg white at 0.5 GPa by Bridgman (1914[link]). However, single crystals of egg-white lysozyme survived a pressure of several gigapascals (Katrusiak & Dauter, 1996[link]; Fourme et al., 2004[link]), which was connected to the concentration of the mother liquor used as the hydrostatic fluid. Cells with externally generated pressures up to about 200 MPa for diffraction measurements on single crystals in a beryllium capsule (Kundrot & Richards, 1986[link]) and on powders contained between beryllium windows (So et al., 1992[link]) have been built. Powder diffraction studies have also been performed on samples frozen under high pressure and recovered to ambient pressure (Gruner, 2004[link]). High-pressure studies can be conveniently performed in the DAC, but because of the usually weak scattering of macromolecular samples, synchrotron radiation is preferred for such experiments (Fourme et al., 2004[link]; Katrusiak & Dauter, 1996[link]).

References

Bridgman, P. W. (1914). The coagulation of albumen by pressure. J. Biol. Chem. 19, 511–512.Google Scholar
Fourme, R. E., Girard, R., Kahn, I., Ascone, M., Mezouar, T., Lin, J. E. & Johnson (2004). State of the art and prospects of macromolecular X-ray crystallography at high hydrostatic pressure. In High-Pressure Crystallography, edited by A. Katrusiak & P. F. McMillan, pp. 527–542. Dordrecht: Kluwer.Google Scholar
Gruner, S. M. (2004). Soft materials and biomaterials under pressure. In High-Pressure Crystallography, edited by A. Katrusiak & P. F. McMillan, pp. 543–556. Dordrecht: Kluwer.Google Scholar
Katrusiak, A. & Dauter, Z. (1996). Compressibility of lysozyme protein crystals by X-ray diffraction. Acta Cryst. D52, 607–608.Google Scholar
Kundrot, C. E. & Richards, F. M. (1986). Collection and processing of X-ray diffraction data from protein crystals at high pressure. J. Appl. Cryst. 19, 208–213.Google Scholar
Royer, C. A. (2002). Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta, 1595, 201–209.Google Scholar
So, P. T. C., Gruner, S. M. & Shyamsunder, E. (1992). Automated pressure and temperature control apparatus for X-ray powder diffraction studies. Rev. Sci. Instrum. 63, 1763–1770.Google Scholar








































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