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

摘要

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.