Structural Features of the Full-Length Adaptor Protein GADS in Solution Determined Using Small-Angle X-Ray Scattering

X-ray diffraction and scattering on a single multipurpose X-ray platform have been used to probe the structure, composition, and thermal behavior of TiO2 nanoparticles ranging in size from 1 to 10 nm. Ambient and non-ambient Bragg diffraction, small-angle X-ray scattering (SAXS), as well as total scattering and pair-distribution function (PDF) analysis are combined to obtain a comprehensive picture of the samples. At these ultrasmall particle-size dimensions, SAXS and PDF prove powerful in distinguishing the salient features of the materials, in particular the size distribution of the primary particles (SAXS) and the identification of the TiO2 polymorphs (PDF). Structural features determined by X-ray scattering techniques are corroborated by high-resolution transmission electron microscopy. The elemental make-up of the materials has been measured using X-ray fluorescence spectrometry and energy-dispersive X-ray analysis.

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Automated microfluidic sample-preparation platform for high-throughput structural investigation of proteins by small-angle X-ray scattering

Journal of Applied Crystallography ◽

10.1107/s0021889811030068 ◽

2011 ◽

Vol 44 (5) ◽

pp. 1090-1099 ◽

Cited By ~ 23

Author(s):

Josiane P. Lafleur ◽

Detlef Snakenborg ◽

Søren S. Nielsen ◽

Magda Møller ◽

Katrine N. Toft ◽

...

Keyword(s):

Sample Preparation ◽

High Throughput ◽

Small Angle ◽

Structural Investigation ◽

Adaptor Protein ◽

Complete Analysis ◽

Uv Absorbance ◽

X Ray ◽

X Ray Scattering ◽

Ray Scattering

A new microfluidic sample-preparation system is presented for the structural investigation of proteins using small-angle X-ray scattering (SAXS) at synchrotrons. The system includes hardware and software features for precise fluidic control, sample mixing by diffusion, automated X-ray exposure control, UV absorbance measurements and automated data analysis. As little as 15 µl of sample is required to perform a complete analysis cycle, including sample mixing, SAXS measurement, continuous UV absorbance measurements, and cleaning of the channels and X-ray cell with buffer. The complete analysis cycle can be performed in less than 3 min. Bovine serum albumin was used as a model protein to characterize the mixing efficiency and sample consumption of the system. The N2 fragment of an adaptor protein (p120-RasGAP) was used to demonstrate how the device can be used to survey the structural space of a protein by screening a wide set of conditions using high-throughput techniques.

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On the nanostructure of radiation-amorphized zircon and pyrochlores: a small-angle x-ray scattering study

Zeitschrift für Kristallographie - Crystalline Materials ◽

10.1524/zkri.220.8.748.67082 ◽

2005 ◽

Vol 220 (8) ◽

Author(s):

Susana Ríos ◽

Christopher M. Martin ◽

Karl R. Whittle

Keyword(s):

Small Angle ◽

Annealing Temperature ◽

Characteristic Length ◽

Structural Features ◽

Density Fluctuations ◽

X Ray ◽

X Ray Scattering ◽

Scattering Study ◽

Electron Density Fluctuations ◽

Ray Scattering

AbstractNanoscale structural features of amorphous zircon and pyrochlore produced by self-irradiation induced amorphization have been characterized by small-angle X-ray scattering (SAXS). Electron density fluctuations were observed in the untreated samples and studied as a function of annealing temperature (up to 1300 °C). In untreated zircon, density fluctuations were found to have a characteristic length-scale of approximately 1 nanometer diameter. A clear scattering maximum develops at ∼3 nm

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Low-Resolution Structure of the Full-Length Barley (Hordeum vulgare) SGT1 Protein in Solution, Obtained Using Small-Angle X-Ray Scattering

PLoS ONE ◽

10.1371/journal.pone.0093313 ◽

2014 ◽

Vol 9 (4) ◽

pp. e93313 ◽

Cited By ~ 4

Author(s):

Michał Taube ◽

Joanna R. Pieńkowska ◽

Artur Jarmołowski ◽

Maciej Kozak

Keyword(s):

Hordeum Vulgare ◽

Small Angle ◽

Full Length ◽

Low Resolution ◽

X Ray ◽

X Ray Scattering ◽

Resolution Structure ◽

Ray Scattering

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Distinctive Low-Resolution Structural Features of Dimers of Antibody–Drug Conjugates and Parent Antibody Determined by Small-Angle X-ray Scattering

Molecular Pharmaceutics ◽

10.1021/acs.molpharmaceut.9b00792 ◽

2019 ◽

Vol 16 (12) ◽

pp. 4902-4912

Author(s):

Didier Law-Hine ◽

Sergii Rudiuk ◽

Audrey Bonestebe ◽

Romain Ienco ◽

Sylvain Huille ◽

...

Keyword(s):

Small Angle ◽

Structural Features ◽

Low Resolution ◽

X Ray ◽

Antibody Drug Conjugates ◽

Drug Conjugates ◽

X Ray Scattering ◽

Antibody Drug ◽

Ray Scattering

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Nanocomposites of Au/Disentangled UHMWPE: A Combined Optical and Structural Study

Molecules ◽

10.3390/molecules25143225 ◽

2020 ◽

Vol 25 (14) ◽

pp. 3225

Author(s):

Stavros X. Drakopoulos ◽

Oreste Tarallo ◽

Linlin Guan ◽

Ignacio Martin-Fabiani ◽

Sara Ronca

Keyword(s):

Gold Nanoparticles ◽

Small Angle ◽

Near Infrared ◽

Polarized Light ◽

Structural Features ◽

X Ray ◽

Optical Absorbance ◽

Entanglement Density ◽

X Ray Scattering ◽

Ray Scattering

The term disentangled refers to polymers with fewer entanglements in the amorphous regions, a metastable condition that can significantly affect the material’s properties and processing behavior. The lower entanglement density in ultra-high molecular weight polyethylene (dis-UHMWPE) facilitates the solid-state processability into uniaxially-oriented specimens reaching very high draw ratios and crystallinities. In this study, Au/dis-UHMWPE nanocomposites were formulated and processed at variable draw ratios. Polarized light microscopy suggests gold nanoparticles are oriented in arrays following the drawing of polymer chains. The structural features, upon orientation, are studied by means of Raman spectroscopy, wide- and small-angle X-ray scattering, and near-infrared spectrophotometry. Crystallinity is found to increase by 15%, as calculated by wide-angle X-ray scattering. The change in optical absorbance in the visible spectrum indicates that, with orientation, the average size of gold aggregates increases, supported quantitatively by small-angle X-ray scattering. Since the gold nanoparticles are expected to be found within amorphous chain segments, the aforementioned findings are attributed to the increase of crystallinity and thus the decrease of available (amorphous) space.

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