X-ray Crystallography at High Pressure to Probe Conformational Fluctuations in Biological Macromolecules

Journal Article · Fri Jan 19 00:00:00 EST 2007 · AIP Conference Proceedings

DOI:https://doi.org/10.1063/1.2436439· OSTI ID:21043388

Girard, Eric; Fourme, Roger ^[1]; Kahn, Richard ^[2]; Dhaussy, Anne-Claire ^[3]; Ascone, Isabella ^[1]; Mezouar, Mohamed ^[4]

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1. Synchrotron-SOLEIL, BP48 Saint Aubin, 91192 Gif sur Yvette (France)
2. IBS, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
3. CRISMAT ENSICAEN, Bd Marechal Juin, 14000, Caen (France)
4. ESRF, BP220, 38027 Grenoble (France)

Macromolecular crystals can be compressed hydrostatically at room temperature in a diamond anvil cell. The quality of diffraction data recorded on the ESRF ID30/ID27 beamlines using a parallel X-ray beam of ultra-short wavelength can meet usual standards. The 3D structures of proteins (monomeric, dimeric and tetrameric) and of a virus have been refined both at atmospheric and at high pressure. High pressure is a way to explore the high energy landscape of macromolecular systems, from the fully folded state to the unfolded state. High energy conformers of biological significance can be selected and trapped under high pressure.

• OSTI ID: 21043388
• Journal Information: AIP Conference Proceedings, Vol. 879, Issue 1; Conference: 9. international conference on synchrotron radiation instrumentation, Daegu (Korea, Republic of), 28 May - 2 Jun 2006; Other Information: DOI: 10.1063/1.2436439; (c) 2007 American Institute of Physics; Country of input: International Atomic Energy Agency (IAEA); ISSN 0094-243X
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
CRYSTALS
DIAMONDS
EUROPEAN SYNCHROTRON RADIATION FACILITY
FLUCTUATIONS
PROBES
PROTEINS
TRAPPING
VIRUSES
WAVELENGTHS
X RADIATION
X-RAY DIFFRACTION