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Small‐angle solution scattering using the mixed‐mode pixel array detector
Author(s) -
Koerner Lucas J.,
Gillilan Richard E.,
Green Katherine S.,
Wang Suntao,
Gruner Sol M.
Publication year - 2011
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s0909049510045607
Subject(s) - small angle x ray scattering , pixel , scattering , detector , optics , physics , noise (video) , materials science , small angle scattering , sampling (signal processing) , dot pitch , computer science , artificial intelligence , image (mathematics)
Solution small‐angle X‐ray scattering (SAXS) measurements were obtained using a 128 × 128 pixel X‐ray mixed‐mode pixel array detector (MMPAD) with an 860 µs readout time. The MMPAD offers advantages for SAXS experiments: a pixel full‐well of >2 × 10 7 10 keV X‐rays, a maximum flux rate of 10 8  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 × 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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