Journal
RADIATION PHYSICS AND CHEMISTRY
Volume 71, Issue 3-4, Pages 905-916Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.radphyschem.2004.04.121
Keywords
structural biology; time resolved X-ray diffraction; X-ray free electron laser
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Recent developments in X-ray source technology provide new opportunities for both the rapid imaging of macromolecules in three dimensions, and the observation of short-lived structural intermediates in light-sensitive macromolecules. Pioneering time-resolved X-ray diffraction studies on macromolecules have laid the foundations for similar studies on increasingly complex macromolecular systems at developing X-ray sources. In addition, the increased peak brilliance expected from an X-ray free electron laser source opens the possibility of new imaging technologies for determining X-ray structures from systems which do not readily yield well-diffracting crystals. Here we review the potential impact of extreme brilliance free electron laser X-ray sources on structural biology. We both sketch the biological case for sub-picosecond X-ray studies of light-sensitive proteins and describe the new imaging possibilities which will emerge through ultrafast X-ray imaging. A central issue is that of X-ray-induced radiation damage on macromolecular samples, and the advantages in this context of working in the femtosecond regime, are discussed. (C) 2004 Elsevier Ltd. All rights reserved.
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