New method to model x-ray scattering from random rough surfaces

2003 ◽  
Author(s):  
Ping Zhao ◽  
Leon P. Van Speybroeck
Keyword(s):  
Rough Surfaces ◽  
New Method ◽  
X Ray ◽  
X Ray Scattering ◽  
Random Rough Surfaces ◽  
Ray Scattering

X-ray scattering from magnetically and structurally rough surfaces

1999 ◽  
Vol 198-199 ◽  
pp. 698-702 ◽  
Author(s):  
R.M. Osgood III ◽  
S.K. Sinha ◽  
J.W. Freeland ◽  
Y.U. Idzerda ◽  
S.D. Bader
Keyword(s):  
Rough Surfaces ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals New Method for Analyzing the Periodic Structure of Multilayer by Differential Anomalous Small-Angle X-ray Scattering

1995 ◽  
Vol 36 (3) ◽  
pp. 408-412 ◽  
Author(s):  
K. Kato ◽  
E. Matsubara ◽  
M. Saito ◽  
T. Kosaka ◽  
Y. Waseda ◽  
...  
Keyword(s):  
Periodic Structure ◽  
Small Angle ◽  
New Method ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Determination of the Height-Height Correlation Function of Rough Surfaces from Diffuse X-Ray Scattering

1995 ◽  
Vol 32 (4) ◽  
pp. 331-336 ◽  
Author(s):  
T Salditt ◽  
T. H Metzger ◽  
J Peisl ◽  
B Reinker ◽  
M Moske ◽  
...  
Keyword(s):  
Correlation Function ◽  
Rough Surfaces ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Background correction of the SAXS intensities scattered by semicrystalline materials

1992 ◽  
Vol 25 (5) ◽  
pp. 646-647 ◽  
Author(s):  
C. Meng
Keyword(s):  
Amorphous Phase ◽  
Small Angle ◽  
Transition Layer ◽  
Amorphous State ◽  
Background Correction ◽  
New Method ◽  
X Ray ◽  
X Ray Scattering ◽  
Nylon 1010 ◽  
Ray Scattering

A new method of background correction of small-angle X-ray scattering (SAXS) intensities scattered by semicrystalline materials is proposed. The intensities scattered by the sample when in the amorphous state were taken as the background scattering. This method was applied to background correction of the SAXS intensities scattered by aged nylon 1010 and the width of the transition layer between crystalline and amorphous phase was determined to be 2.0 nm.

Differential ultracentrifugation coupled to small-angle X-ray scattering on macromolecular complexes

2015 ◽  
Vol 48 (3) ◽  
pp. 769-775 ◽  
Author(s):  
Robert M. G. Hynson ◽  
Anthony P. Duff ◽  
Nigel Kirby ◽  
Stephan Mudie ◽  
Lawrence K. Lee
Keyword(s):  
Small Angle ◽  
Quaternary Structure ◽  
Protein Complexes ◽  
New Method ◽  
Size Exclusion ◽  
Saxs Data ◽  
X Ray ◽  
X Ray Scattering ◽  
Macromolecular Protein ◽  
Ray Scattering

Small-angle X-ray scattering (SAXS) can provide accurate structural information and low-resolution shapes of macromolecules in solution. The technique is particularly amenable to large protein assemblies, which produce a strong scattering signal. Hence, SAXS can be a powerful tool to elucidate quaternary structure, especially when used in combination with high-resolution structural techniques such as X-ray crystallography and NMR. Sample requirements for SAXS experiments are stringent and only monodispersed samples can be satisfactorily analysed. Often, it is not possible to obtain a stable monodispersed sample of the protein of interest, in particular for multi-subunit protein complexes. In these circumstances, when the complex is less than approximately 1 MDa, size exclusion chromatography (SEC) coupled with SAXS (SEC-SAXS) can facilitate the separation of monodispersed protein from a polydispersed sample for a sufficient amount of time to collect useful SAXS data. However, many very large multi-subunit macromolecular assemblies have not been successfully purified with SEC, and hence despite being well suited to SAXS there is often no way to produce sample of sufficient quality. Rather than SEC, differential ultracentrifugation (DU) is the method of choice for the final step in the purification of large macromolecular protein complexes. Here, a new method is described for collecting SAXS data on samples directly from the fractionated elution of ultracentrifuge tubes after DU. It is demonstrated using apoferritin as a model protein that, like SEC-SAXS, DU-coupled SAXS can facilitate simultaneous purification and data collection. It is envisaged that this new method will enable high-quality SAXS data to be collected on a host of large macromolecular protein complex assemblies for the first time.

Microbeam grazing incidence small angle X-ray scattering—a new method to investigate heterogeneous thin films and multilayers

2004 ◽  
Vol 59 (10-11) ◽  
pp. 1765-1773 ◽  
Author(s):  
S.V. Roth ◽  
P. Müller-Buschbaum ◽  
M. Burghammer ◽  
H. Walter ◽  
P. Panagiotou ◽  
...  
Keyword(s):  
Thin Films ◽  
Small Angle ◽  
Grazing Incidence ◽  
New Method ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering
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