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11 citations found for Liao, P.

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Acta Cryst. (2017). A73, C1267
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Methods for purifying and crystallizing the precursors and autoprocessed enzymes of glycosylasparaginase are reported. The mutant precursors are active in autoproteolysis but have much slower rates.

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Acta Cryst. (2011). A67, C140-C141
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The bond lengths and mol­ecular conformation of the title compound, C17H22N2O5S2, can be correlated with electronic conjugation and steric effects.

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In the title compound, C10H15N3O3, the mol­ecules form dimeric associations via inversion-generated pairs of N—H...O hydrogen bonds.

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Temperature (20–300 K)- and energy-dependent phase shifts of resonant multiple-beam X-ray diffraction in germanium crystals, involving forbidden (002) and weak (222) reflections, are reported.

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Acta Cryst. (2014). A70, C391
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We have used resonant multi-beam diffraction with the primary reflections G=(h/2 h/2 0) and G=(h/4 h/4 0) (h is an odd number) to investigate the charge ordering and Jahn-Teller distortion, respectively, in La0.5Sr1.5MnO4 low temperature phase. While the Renninger scans with G=(h/2 h/2 0) shows several Aulfhellung-type four-beam diffraction, most of the multi-beam diffraction with G=(h/4 h/4 0) has an Umweganregung-type nature. A detailed study of multi-beam diffraction anomalous fine structure (M-DAFS) of (0 0 0)/(3/2 3/2 0)/(1 -1 0)/(5/2 1/2 0) OUT diffraction is carried out. Its triplet invariant phase approach 1800 when the x-ray energy is tuned away from manganese K-edge, and approach 900 when the x-ray energy is tuned on manganese K-edge. In other words, its multi-beam diffraction profile shows strong asymmetry when (3/2 3/2 0) diffraction intensity is dominated by Jahn-Teller distortion, and becomes more symmetric when charge ordering dominated. This characteristic can be successfully simulated by tensor form dynamical x-ray diffraction theory accompanied with FDMNES software [1] calculations.

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Sinusoidal wave type distortions of La0.5Sr1.5MnO4 in the low-temperature orthorhombic phase were observed using multi-beam resonant X-ray diffraction and dynamical theory.

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Acta Cryst. (2014). A70, C1322
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Spider dragline silk is one of the strongest nature fibers and some of their features are even better than those of the best synthetic fibers. Understanding the mechanisms inducing silk variability may have implications for biomimetics and the synthesis of environmentally responsive materials. Dragline silk contains both elasticity (amorphous) and crystalline regions. Our previous studies had demonstrated that spiders might vary the protein composition and thus physical properties of silks when experiencing food with different nutrient level. In this study we fed Nephila pilipes with high, low and no protein foods and collected their dragline silks for synchrotron Radiation (SR) wide-angle X-ray scattering (WAXS) and small-angle X-ray scattering (SAXS) examinations. The WAXS data showed a significant difference in crystalline fractions of dragline silks produced by N. pilipes experiencing different food treatments. In addition, the orientation of crystallines also varied considerably among silks produced by spiders in three treatment groups. The SAXS data, obtained with the beam incident along and perpendicular to the fiber axis revealed a mesostructure comprising nano crystallites (beta sheets) stack spirally along the spider fibril axis. Such results indicate that spiders experiencing different nutrient stress level might produce dragline silks of different physical properties due to variations in crystalline density, orientation and the meso-phase structures in nano scale. Furthermore, varying environmental wind strength leads to changes in tensile mechanics of spider dragline silk hence produced. Exposing the spider Cyclosa mulmeinensis to controlled stress from constant airflow, we found correlated changes in (i) amino acid composition, (ii) tensile mechanics and (iii) crystallinity, of the dragline silk; which results suggest that protein variation and/or post secretion crystalline variations are associated with the mechanical properties of the spider silks.


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Acta Cryst. (2017). A73, C551
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