Spatial correlation functions of radially distributed quantities applied to small-angle scattering

Vass, Sz.

doi:10.1107/s0108767397016693

Cited by 4 publications

(4 citation statements)

References 8 publications

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“…33 For X-ray patterns from a Kratky camera the ITP program 34 is the appropriate tool for determining p(r) in a model-free way with mathematical rigor. The results are plotted together with p(r) functions calculated 35 from the 2S-(Figure 3) and 4C model form factors (Figure 4). The first peak in the experimental p(r) function stands for the micellar core and seems to be approximated slightly better by the 2S model.…”

Section: Fitting Model Functionsmentioning

confidence: 99%

Models of Micellar Structure Tested by SANS and SAXS (from a Kratky Camera) in Cesium Dodecyl Sulfate Solution

Vass

Pleštil²,

Laggner

et al. 2003

J. Phys. Chem. B

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Small-angle neutron- (SANS) and X-ray-scattering (SAXS) patterns obtained at 40 °C from 0.0729 m D2O solution of cesium dodecyl sulfate (CsDDS) have been simultaneously evaluated in terms of the conventional two-shell model, a three-shell model created for demonstration purposes, and a newly developedand partly testedfour-component model. The simultaneous fitting is based on the fact that the two types of coherent scattering patterns differ only in the neutron- and X-ray scattering lengths. For comparison, the SANS and SAXS patterns were evaluated separately, too. In contrast to the two- and three-shell models, the four-component model is able to represent the continuously varying spatial distribution of the scattering contrast. From the results, it seems that the most reliable data are obtained from fitting the four-component model simultaneously to both patterns. Along with (approximate) core- and counterion profiles, application of the latter model can result in the spatial distribution of the solvent molecules around the micellar center. If an atom or a molecular group has well-distinguishable scattering contrast relative to both types of scattering (such as Cs+ counter-, and -SO4 -- headgroup-ions), utilization of the four-component model enables their molecular volumes to be treated as variable model parameters, thus providing a unique method for determining their hydration properties in a structured nonsimple liquid.

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Section: Fitting Model Functionsmentioning

confidence: 99%

Models of Micellar Structure Tested by SANS and SAXS (from a Kratky Camera) in Cesium Dodecyl Sulfate Solution

Vass

Pleštil²,

Laggner

et al. 2003

J. Phys. Chem. B

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“…The cross-correlation function of quantities f1´r1µ and f2´r2µ, distributed radially over spheres of radii R1 and R2, is given by the following integral (Vass, 1998):…”

Section: Correlation Functions Of Radially Distributed Quantitiesmentioning

confidence: 99%

“…Notations for calculating the cross correlation functionf 2 12´r µ of quantities f 1´r1 µ and f 2´r2 µ, distributed radially on spheres of radii R 1 and R 2 , respectively. (Reproduced from Vass, 1998).…”

Section: Figurementioning

confidence: 99%

Distance distribution function of interacting uniform spheres

Vass

2000

J Appl Cryst

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The scattering intensity equals the Fourier-transform of the distance distribution function p´tµ t 2 ∆˜ 2´t µ of the sample, where ∆˜ 2´t µ is the autocorrelation function of the scattering contrast ∆ ´rµ. ∆˜ 2´t µ carries information both on the structure of the elementary scatterers and on their spatial distribution. In the present paper a method is described how to separate the two types of information in a system of interacting hard spheres.

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“…8 As a matter of fact, in this case the associated SAXS curves are free from frequently complex effects due to anisotropy, size polydispersity, and spatial correlation. 7,[9][10][11] Using classical setups, SAXS technique allows for the determination of low-resolution structural parameters of biological systems, such as macromolecules in solution, with sizes ranging from 1 nm up to 50 nm. 1,7 The relevant parameters usually determined for macromolecules from SAXS data are the radius of gyration, R g , threedimensional low-resolution envelope, molecular weight, M r , and oligomeric state.…”

Section: Introductionmentioning

confidence: 99%

SAXSMoW 3.0: New advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale

et al. 2021

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SAXSMoW (SAXS Molecular Weight) is an online platform widely used over the past few years for determination of molecular weights of proteins in dilute solutions. The scattering intensity retrieved from small-angle X-ray scattering (SAXS) raw data is the sole input to SAXSMoW for determination of molecular weights of proteins in liquid. The current updated SAXSMoW version 3.0 determines the linear dependence of the true protein volume on their apparent protein volume, based on SAXS curves calculated for 67,000 protein structures selected from the Protein Data Bank. SAXSMoW 3.0 was tested against 43 experimental SAXS scattering curves from proteins with known molecular

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Spatial correlation functions of radially distributed quantities applied to small-angle scattering

Cited by 4 publications

References 8 publications

Models of Micellar Structure Tested by SANS and SAXS (from a Kratky Camera) in Cesium Dodecyl Sulfate Solution

Models of Micellar Structure Tested by SANS and SAXS (from a Kratky Camera) in Cesium Dodecyl Sulfate Solution

Distance distribution function of interacting uniform spheres

SAXSMoW 3.0: New advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale

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