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- W2068440260 abstract "The pair-distance distribution function P(r) is a measure of the frequency of interatomic vector lengths within a protein molecule, and can provide information about the shape and intra-structure of the scattering particle. P(r) function has long been recognized as a smooth curve, and the oscillation at low distance is mainly due to unphysical truncation ripples in Fourier transformation.Recently, we have developed an effective method and succeeded in collecting high-quality SAXS and WAXS of protein solutions, showing negligible radiation damage (1) (2) (3). A high resolution pair-distance distribution function, P(r), of protein molecules has been obtained from the complete solution scattering curve made by combining accurate small-angle and wide-angle X-ray scattering data out to crystallographic resolution (2 A).Both indirect and direct Fourier transforms exhibit two distinct peaks at 1.4 A and 5.1 A in P(r). X-ray crystallographic data demonstrate that these peaks correspond to two intramolecular distances: the average bond length between C, N and O atoms and the pitch of an α-helix, respectively. Hence some high resolution aspects of the structure and function of a protein can be investigated in solution.Reference:1. X. Hong and Q. Hao. 2009. Measurements of accurate x-ray scattering data of protein solutions using small stationary sample cells. Review of Scientific Instruments 80:014303.2. X. Hong and Q. Hao. 2009. High resolution pair-distance distribution function P(r) of protein solutions. APPLIED PHYSICS LETTERS 94:083903-083903.3. X. Hong and Q. Hao. 2009. Combining solution wide-angle X-ray scattering and crystallography: determination of molecular envelope and heavy-atom sites. Journal of Applied Crystallography 42:259-264." @default.
- W2068440260 created "2016-06-24" @default.
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- W2068440260 date "2010-01-01" @default.
- W2068440260 modified "2023-09-29" @default.
- W2068440260 title "Pair-Distance Distribution Function P(R) of Protein Solution at Crystallographic Resolution" @default.
- W2068440260 doi "https://doi.org/10.1016/j.bpj.2009.12.947" @default.
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