Small angle neutron and x-ray scattering studies of concentrated protein solutions II. Cytochrome C

Biopolymers ◽  
1988 ◽  
Vol 27 (7) ◽  
pp. 1065-1083 ◽  
Author(s):  
Chuan-Fu Wu ◽  
Sow-Hsin Chen
2007 ◽  
Vol 40 (2) ◽  
pp. 218-231 ◽  
Author(s):  
Giuseppe Portale ◽  
Alessandro Longo ◽  
Lucio D'Ilario ◽  
Andrea Martinelli ◽  
Ruggero Caminiti ◽  
...  

The use of polychromaticBremsstrahlungX-rays generated by commercial tubes for energy-dispersive small-angle scattering measurements has not been extensively discussed in the literature, mainly because of some difficulties associated with it. If a suitable experimental setup is chosen and concomitant phenomena are taken into account for correcting the observed X-ray patterns, energy-dispersive small-angle X-ray scattering (SAXS) may become an interesting alternative to conventional measurements based on monochromatic beams. Energy-dispersive SAXS experiments carried out on protein solutions, micelles, semicrystalline polymers and catalytic systems are discussed to illustrate the new opportunities offered by this technique as well as its limitations.


Biochemistry ◽  
1988 ◽  
Vol 27 (4) ◽  
pp. 1121-1125 ◽  
Author(s):  
Jill Trewhella ◽  
Vanice A. P. Carlson ◽  
Elizabeth H. Curtis ◽  
Douglas B. Heidorn

2018 ◽  
Vol 25 (4) ◽  
pp. 1113-1122 ◽  
Author(s):  
Martin A. Schroer ◽  
Clement E. Blanchet ◽  
Andrey Yu. Gruzinov ◽  
Melissa A. Gräwert ◽  
Martha E. Brennich ◽  
...  

Radiation damage by intense X-ray beams at modern synchrotron facilities is one of the major complications for biological small-angle X-ray scattering (SAXS) investigations of macromolecules in solution. To limit the damage, samples are typically measured under a laminar flow through a cell (typically a capillary) such that fresh solution is continuously exposed to the beam during measurement. The diameter of the capillary that optimizes the scattering-to-absorption ratio at a given X-ray wavelength can be calculated a priori based on fundamental physical properties. However, these well established scattering and absorption principles do not take into account the radiation susceptibility of the sample or the often very limited amounts of precious biological material available for an experiment. Here it is shown that, for biological solution SAXS, capillaries with smaller diameters than those calculated from simple scattering/absorption criteria allow for a better utilization of the available volumes of radiation-sensitive samples. This is demonstrated by comparing two capillary diameters d i (d i = 1.7 mm, close to optimal for 10 keV; and d i = 0.9 mm, which is nominally sub-optimal) applied to study different protein solutions at various flow rates. The use of the smaller capillaries ultimately allows one to collect higher-quality SAXS data from the limited amounts of purified biological macromolecules.


2016 ◽  
Vol 23 (2) ◽  
pp. 480-486 ◽  
Author(s):  
D. C. F. Wieland ◽  
V. M. Garamus ◽  
T. Zander ◽  
C. Krywka ◽  
M. Wang ◽  
...  

The development of a dedicated small-angle X-ray scattering setup for the investigation of complex fluids at different controlled shear conditions is reported. The setup utilizes a microfluidics chip with a narrowing channel. As a consequence, a shear gradient is generated within the channel and the effect of shear rate on structure and interactions is mapped spatially. In a first experiment small-angle X-ray scattering is utilized to investigate highly concentrated protein solutions up to a shear rate of 300000 s−1. These data demonstrate that equilibrium clusters of lysozyme are destabilized at high shear rates.


2002 ◽  
Vol 99 (3) ◽  
pp. 1329-1334 ◽  
Author(s):  
S. Akiyama ◽  
S. Takahashi ◽  
T. Kimura ◽  
K. Ishimori ◽  
I. Morishima ◽  
...  

2018 ◽  
Vol 63 (5) ◽  
pp. 713-718
Author(s):  
A. M. Popov ◽  
A. S. Boikova ◽  
V. V. Volkov ◽  
Yu. A. D’yakova ◽  
K. B. Il’ina ◽  
...  

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