Journal
JOURNAL OF SYNCHROTRON RADIATION
Volume 18, Issue -, Pages 148-156Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0909049510045607
Keywords
small-angle X-ray scattering; detector development
Categories
Funding
- US NIH [RR001646, RR014613]
- US DOE [DE-FG02-97ER62443]
- CHESS
- US NSF
- NIH-NIGMS through NSF [DMR-0225180]
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Solution small-angle X-ray scattering (SAXS) measurements were obtained using a 128 x 128 pixel X-ray mixed-mode pixel array detector (MMPAD) with an 860 mu s readout time. The MMPAD offers advantages for SAXS experiments: a pixel full-well of > 2 x 107 10 keV X-rays, a maximum flux rate of 108 X-rays pixel-1 s-1, and a sub-pixel point-spread function. Data from the MMPAD were quantitatively compared with data from a charge-coupled device (CCD) fiber-optically coupled to a phosphor screen. MMPAD solution SAXS data from lysozyme solutions were of equal or better quality than data captured by the CCD. The read-noise (normalized by pixel area) of the MMPAD was less than that of the CCD by an average factor of 3.0. Short sample-to-detector distances were required owing to the small MMPAD area (19.2 mm x 19.2 mm), and were revealed to be advantageous with respect to detector read-noise. As predicted by the Shannon sampling theory and confirmed by the acquisition of lysozyme solution SAXS curves, the MMPAD at short distances is capable of sufficiently sampling a solution SAXS curve for protein shape analysis. The readout speed of the MMPAD was demonstrated by continuously monitoring lysozyme sample evolution as radiation damage accumulated. These experiments prove that a small suitably configured MMPAD is appropriate for time-resolved solution scattering measurements.
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