Abstract
To bridge the gap between traditional multilayer and crystal optics a high-resolution multilayer monochromator with a bandwidth of 0.22% has been designed and installed on a bending-magnet beamline (F3) at the Cornell High Energy Synchrotron Source (CHESS) to provide an unfocused monochromatic X-ray beam for protein crystallography experiments. Crystallographic data of excellent quality from a medium-sized protein, Concanavalin A, were collected and processed using standard Crystallographic programs. The data were successfully used for a structure solution and refinement. The flux from the multilayer monochromator is enhanced, relative to that from a flat Si(111) monochromator, by a factor of 5; consequently, data collection is faster and/or smaller samples may be used. At the same time, the bandwidth is narrow enough to avoid streaked spots. This experiment suggests that multilayer optics may play a valuable role in satisfying the demands of the structural biology community for rapid X-ray data collection, particularly at under-utilized bending-magnet beamlines.
Original language | English (US) |
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Pages (from-to) | 345-348 |
Number of pages | 4 |
Journal | Journal of Synchrotron Radiation |
Volume | 12 |
Issue number | 3 |
DOIs | |
State | Published - May 2005 |
Keywords
- Macromolecular crystallography
- Monochromators
- Multilayer optics
- Protein crystallography
- X-ray optics
ASJC Scopus subject areas
- Radiation
- Nuclear and High Energy Physics
- Instrumentation