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
Keyword(s):  
Cytochrome C ◽  
Small Angle ◽  
Protein Solutions ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Small-angle energy-dispersive X-ray scattering using a laboratory-based diffractometer with a conventional source

2007 ◽  
Vol 40 (2) ◽  
pp. 218-231 ◽  
Author(s):  
Giuseppe Portale ◽  
Alessandro Longo ◽  
Lucio D'Ilario ◽  
Andrea Martinelli ◽  
Ruggero Caminiti ◽  
...  
Keyword(s):  
Small Angle ◽  
Energy Dispersive ◽  
Protein Solutions ◽  
X Rays ◽  
Catalytic Systems ◽  
X Ray ◽  
X Ray Scattering ◽  
Angle Scattering ◽  
Ray Patterns ◽  
Ray Scattering

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.

Differences in the solution structures of oxidized and reduced cytochrome c measured by small-angle x-ray scattering

Biochemistry ◽  
1988 ◽  
Vol 27 (4) ◽  
pp. 1121-1125 ◽  
Author(s):  
Jill Trewhella ◽  
Vanice A. P. Carlson ◽  
Elizabeth H. Curtis ◽  
Douglas B. Heidorn
Keyword(s):  
Cytochrome C ◽  
Small Angle ◽  
X Ray ◽  
Solution Structures ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Smaller capillaries improve the small-angle X-ray scattering signal and sample consumption for biomacromolecular solutions

2018 ◽  
Vol 25 (4) ◽  
pp. 1113-1122 ◽  
Author(s):  
Martin A. Schroer ◽  
Clement E. Blanchet ◽  
Andrey Yu. Gruzinov ◽  
Melissa A. Gräwert ◽  
Martha E. Brennich ◽  
...  
Keyword(s):  
Small Angle ◽  
A Priori ◽  
Protein Solutions ◽  
Biological Macromolecules ◽  
Saxs Data ◽  
X Ray ◽  
X Ray Scattering ◽  
A Cell ◽  
Flow Through ◽  
Ray Scattering

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.

scholarly journals Studying solutions at high shear rates: a dedicated microfluidics setup

2016 ◽  
Vol 23 (2) ◽  
pp. 480-486 ◽  
Author(s):  
D. C. F. Wieland ◽  
V. M. Garamus ◽  
T. Zander ◽  
C. Krywka ◽  
M. Wang ◽  
...  
Keyword(s):  
Shear Rate ◽  
Small Angle ◽  
Protein Solutions ◽  
High Shear ◽  
X Ray ◽  
Shear Rates ◽  
X Ray Scattering ◽  
High Shear Rates ◽  
Shear Gradient ◽  
Ray Scattering

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.

scholarly journals Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering

2002 ◽  
Vol 99 (3) ◽  
pp. 1329-1334 ◽  
Author(s):  
S. Akiyama ◽  
S. Takahashi ◽  
T. Kimura ◽  
K. Ishimori ◽  
I. Morishima ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Small Angle ◽  
X Ray ◽  
X Ray Scattering ◽  
Conformational Landscape ◽  
Ray Scattering

Microfluidic Cell for Studying the Precrystallization Stage Structure of Protein Solutions by Small-Angle X-Ray Scattering

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 ◽  
...  
Keyword(s):  
Small Angle ◽  
Stage Structure ◽  
Protein Solutions ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering
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