14 October 2005 Amorphous silicon based direct x-ray conversion detector for protein structure analysis
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Abstract
Detailed knowledge of protein structure is vital to the understanding of numerous biological processes and to expedite advancements in pharmaceutical research. The atomic structure of protein can be determined by measuring the intensity of its X-ray diffraction pattern. The functional wavelength of X-ray for this purpose lies in the range of 0.01-1 nm. The diffraction pattern produced by X-ray of such wavelength can be read by a large area (~ 20 cm x 20 cm) detector. The detector should have good spatial resolution (FWHM ~ 2 pixels) to detect every Bragg peak in the pattern. In addition, a wide dynamic range (~106) is desirable to accurately measure the intensity of Bragg peaks. Amorphous silicon (a-Si:H) based detector is a potential candidate to meet these requirements; in particular, it is attractive by virtue of its inexpensive manufacturing process and large area compatibility compared to the existing CCD and image plate based detection techniques. In this work, we investigate by modeling the feasibility of an a-Si:H based detector for the study of protein structure. The proposed detector employs amorphous selenium (a-Se) photoconductor layer to directly convert the incident X-ray to a charge image, which is then electronically read by an array of a-Si:H thin film transistors. The modeling results show that the detector reasonably satisfies the requirements for determination of protein.
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Afrin Sultana, Arokia Nathan, J. A. Rowlands, "Amorphous silicon based direct x-ray conversion detector for protein structure analysis", Proc. SPIE 5969, Photonic Applications in Biosensing and Imaging, 596928 (14 October 2005); doi: 10.1117/12.629543; https://doi.org/10.1117/12.629543
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