A fluorescent X-ray interference method can effectively measure nanometer-level conformational changes for non-crystallized molecules and proteins in aqueous conditions. The time-resolved technique can be used to obtain information about the dynamics of molecules and proteins. Instrumentation for time-resolved fluorescent X-ray interference has been designed. A typical interference-fringe pattern was observed with approximately 3 s of X-ray exposure time from K-fluorescent X-rays emitted from a Zn monoatomic layer on an Rh substrate. The primary X-ray beam was polychromed with a mirror for total external reflection of X-rays and was tuned to an energy level at which only Zn K radiation became optimally excited. The glancing angle of the primary X-ray beam was fixed at a glancing angle at which the total intensity of K-fluorescent X-rays emitted from Zn atoms corresponded to the maximum value. The fluorescent X-ray interference fringes were monitored with an imaging plate (IP) as a non-energy-dispersive two-dimensional detector. The exposed interference fringes on the IP were integrated along the direction of the fringes. The integrated fringes were in close agreement with a theoretical estimate based on the interference among transmitted and reflected waves at interfaces in the sample.
- Fluorescent X-ray interference
- Imaging plates
- Polychromatic primary beam
- Time-resolved technique
ASJC Scopus subject areas
- Nuclear and High Energy Physics