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Résumé |
Until recently, only two crystal structures of small proteins at high pressure below 200 MPa generated in a Be cell were published [1,2]. The lack of structural data at high pressure on macromolecules was due mainly to the cumulated complexities of high-pressure containment and crystallography. A technical breakthrough was achieved with a set-up at the ESRF ID30/ID27 beamline combining a diamond anvil cell, ultra-short wavelength (0.33 Å) X-rays from undulators and a large imaging plate [3]. The accessible pressure range was increased by nearly one order of magnitude. The quality of diffraction data collected under high pressure achieved usual standards.
After a brief introduction about the interest of high pressure in biology and about the specificity of macromolecular crystals, I will present some of the technical advances as well as some of the scientific results that we obtained [4,5]. Among these results, I will focus on the behaviour under pressure of a virus particle, a tetrameric protein as well as a small part of DNA, thus demonstrating that high pressure macromolecular crystallography can now be considered as a mature and general technique.
[1] Kundrot C.E. & Richards F.M., 1987, J. Mol. Biol., 193, 157.
[2] Urayama P., Phillips G.N. & Gruner S.M., 2002, Structure, 10, 51
[3] Fourme R. et al., 2003, Acta Cryst., D59, 1767.
[4] Girard E., et al 2005, Biophys. J., 88, 3562.
[5] Colloc'h N., et al, 2006, Biochim. Biophys. Acta, 1764, 391.
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