scholarly journals Small-angle X-ray scattering (SAXS) studies of the low-resolution structure of the ribosomal GTPase EFL1, the SBDS protein and their complex

2016 ◽  
Vol 72 (a1) ◽  
pp. s180-s181 ◽  
Author(s):  
Dritan Siliqi ◽  
Davide Altamura ◽  
Abril Gijsbers ◽  
Eugenio de la Mora ◽  
Cinzia Giannini ◽  
...  
2020 ◽  
Author(s):  
Tyler Mrozowich ◽  
Amy Henrickson ◽  
Borries Demeler ◽  
Trushar R Patel

AbstractViral infections are responsible for numerous deaths worldwide. Flaviviruses, which contain RNA as their genetic material, are one of the most pathogenic families of viruses. There is an increasing amount of evidence suggesting that their 5’ and 3’ non-coding terminal regions are critical for their survival. In this study, the 5’ and 3’ terminal regions of Murray Valley Encephalitis and Powassan virus were examined using biophysical and computational modeling methods. First, the purity of in-vitro transcribed RNAs were investigated using size exclusion chromatography and analytical ultracentrifuge methods. Next, we employed small-angle X-ray scattering techniques to study solution conformation and low-resolution structures of these RNAs, which suggested that the 3’ terminal regions are highly extended, compared to the 5’ terminal regions for both viruses. Using computational modeling tools, we reconstructed 3-dimensional structures of each RNA fragment and compared them with derived small-angle X-ray scattering low-resolution structures. This approach allowed us to further reinforce that the 5’ terminal regions adopt more dynamic structures compared to the mainly double-stranded structures of the 3’ terminal regions.


1992 ◽  
Vol 25 (2) ◽  
pp. 181-191 ◽  
Author(s):  
J. J. Müller ◽  
H. Schrauber

Low-resolution three-parameter models of the shape of a biopolymer in solution can be determined by a new indirect method from small-angle X-ray scattering without contrast-variation experiments. The basic low-resolution model employed is a triaxial ellipsoid – the inertia-equivalent ellipsoid (IEE). The IEE is related to the tensor of inertia of a body and the eigenvalues and eigenvectors of this tensor can be calculated directly from the atomic coordinates and from the homogeneous solvent-excluded body of a molecule. The IEE defines a mean molecular surface (like the sea level on earth) which models the molecular shape adequately if the IEE volume is not more than 30% larger than the dry volume of the molecule. Approximately 10 to 15% of the solvent-excluded volume is outside the ellipsoid; the radii of gyration of the IEE and of the homogeneous molecular body are identical. The largest diameter of the IEE is about 5 to 15% (~0.2–0.8 nm) smaller than the maximum dimension of globular molecules with molecular masses smaller than 65000 daltons. From the scattering curve of a molecule in solution the IEE can be determined by a calibration procedure. 29 proteins of known crystal structure have been used as a random sample. Systematic differences between the axes of the IEE, calculated directly from the structure, and the axes of the scattering-equivalent ellipsoids of revolution, estimated from the scattering curve of the molecule in solution, are used to derive correction factors for the axial dimensions. Distortions of model dimensions of 20 to 40% (up to 1 nm), caused by misinterpretation of scattering contributions from electron density fluctuations within the molecule, are reduced to a quarter by applying these correction factors to the axes of the scattering-equivalent ellipsoids of revolution. In a computer experiment the axes of the inertia-equivalent ellipsoids have been determined for a further nine proteins with the same accuracy. The automated estimation of the IEE from the scattering curve of a molecule in solution is realized by the Fortran77 program AUTOIEE.


2007 ◽  
Vol 40 (s1) ◽  
pp. s229-s234 ◽  
Author(s):  
Jan Lipfert ◽  
Vincent B. Chu ◽  
Yu Bai ◽  
Daniel Herschlag ◽  
Sebastian Doniach

2003 ◽  
Vol 36 (3) ◽  
pp. 503-508 ◽  
Author(s):  
Vladimir V. Volkov ◽  
Viktor A. Lapuk ◽  
Renata L. Kayushina ◽  
Eleonora V. Shtykova ◽  
Elena Yu. Varlamova ◽  
...  

2005 ◽  
Vol 38 (6) ◽  
pp. 996-1003 ◽  
Author(s):  
A. N. Ozerin ◽  
D. I. Svergun ◽  
V. V. Volkov ◽  
A. I. Kuklin ◽  
V. I. Gordelyi ◽  
...  

A low-resolutionab initioshape determination was performed from small-angle neutron and X-ray scattering (SANS and SAXS) curves from solutions of polycarbosilane dendrimers with the three-functional and the four-functional branching centre of the fourth, fifth, sixth, seventh and eighth generations. In all cases, anisometric dendrimer shapes were obtained. The overall shapes of the dendrimers with the three- and four-functional branching centres were oblate ellipsoids of revolution and triaxial ellipsoids, respectively. The restored bead models revealed a pronounced heterogeneity within the dendrimer structure. The density deficit was observed in the central part and close to the periphery of the dendrimers. The fraction of the overall volume of the dendrimers available for solvent penetration was about 0.2–0.3. These results may help in the design of new practical applications of dendrimer macromolecules.


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