An investigation of the structure of Alfalfa mosaic virus by small-angle neutron scattering

Cusack, Stephen; Miller, A.; Krijgsman, P.C.J.; Mellema, J.E.

doi:10.1016/0022-2836(81)90543-x

Cited by 44 publications

(14 citation statements)

References 23 publications

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“…The guessed solution can be simply a parametrized scattering curve, without knowledge of the sample (Schelten and Hossfeld, 1971), but it is of more interest to fit the smeared Fourier transform of the distance-distribution function (Glatter, 1979) or the radial density distribution (e.g. Cusack et al, 1981) of a real-space model to the data.…”

Section: Correction Of Instrumental Effectsmentioning

confidence: 99%

Small‐Angle Scattering of X‐Rays and Neutrons

Williams

May

Guinier

1999

X‐ray Characterization of Materials

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Section: Correction Of Instrumental Effectsmentioning

confidence: 99%

Small‐Angle Scattering of X‐Rays and Neutrons

Williams

May

Guinier

1999

X‐ray Characterization of Materials

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“…It is well known that the finer details of a (Jack and Harrison 1975). For example, for scattering from icosahedral capsids consisting of globular protein, the packing arrangement gives rise to large broad bumps at intermediate values of the scattering vectors (Chauvin et al 1978;Cusack et al 1981). The position of the bump is related to the characteristic distance d between the proteins as q ~ 2 rc/d.…”

Section: Appendix: Deviation From Spherical Symmetrymentioning

confidence: 99%

Structure of clathrin-coated vesicles from small-angle scattering experiments

Pedersen¹

1993

Eur Biophys J

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Previously published small-angle neutron and X-ray scattering data from coated vesicles, reassembled coats, and stripped vesicles have been analyzed in terms of one common model. The neutron data sets include contrast variation measurements at three different D2O solvent concentrations. The model used for interpreting the data has spherical symmetry and explicitly takes into account polydispersity, which is described by a Gaussian distribution. A constant thickness of the clathrin coats is assumed. The fitting of the model shows that the coated vesicles consist of a low-density outer protein shell (clathrin) and a central protein shell (accessory polypeptides and receptors) of approximately six times higher density. For the X-ray scattering and neutron contrast variation data, the polydispersity of the samples is of the order of 90 A (full-width-at-half-maximum value) and the average outer radius is approximately 400 A. The inner high-density shell has inner and outer radii of 115 and 190 A, respectively. A simultaneous fit to the three neutron contrast variation data sets identifies the lipid membrane with a thickness of 40 A and an outer radius of 196 A. Thus, the membrane and the high-density protein shell overlap in space, which shows that the lipid membrane contains protein. The molecular mass of the average particle is 27 x 10(6) Da. The coated vesicles consist, on average, of approximately 85% protein and 15% lipids. About 40% of the protein mass is situated in the central high-density shell, which gives a large amount of protein in the lipid membrane. The densities of the central shell and the lipid membrane show that the hydration is small in the central region. A comparison of the total mass, the mass distribution, and the structure of the average-size particles with the barrel structure shows that the accessory polypeptides are incorporated in the lipid membrane. The results from the neutron data for the reassembled coats show that the structure of these particles is very similar to the structure of the native coats. The main difference is a higher density of the central protein shell, which shows that the membrane is replaced by protein in the reassembled coats.

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“…Systems as varied as the calmodulin-myosin lightchain kinase (MLCK) complex (Krueger et al, 1997(Krueger et al, , 1998, protein kinase A (Zhao et al, 1998;Heller et al, 2004), the GroEL-GroES chaperonin complex (Krueger et al, 2003), the neurolignin-neurexin complex (Comoletti et al, 2007), and a complex involved in histidine kinase inhibition (Whitten et al, 2007) ., 1999), and methionine repressor MetJ-DNA complexes (Augustus et al, 2006). Virus structures are also excellent candidates for SANS with contrast variation studies (Jacrot et al, 1977;Chauvin et al, 1978;Cusack et al, 1981;Kruse et al, 1982;Inoue and Timmins, 1985;Sato et al, 1995;He et al, 2010He et al, , 2012.…”

Section: Applicationsmentioning

confidence: 99%

Neutron Scattering Techniques and Applications in Structural Biology

et al. 2013

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Neutron scattering is exquisitely sensitive to the position, concentration, and dynamics of hydrogen atoms in materials and is a powerful tool for the characterization of structure-function and interfacial relationships in biological systems. Modern neutron scattering facilities offer access to a sophisticated, nondestructive suite of instruments for biophysical characterization that provides spatial and dynamic information spanning from Ångstroms to microns and from picoseconds to microseconds, respectively. Applications in structural biology range from the atomic-resolution analysis of individual hydrogen atoms in enzymes through to meso- and macro-scale analysis of complex biological structures, membranes, and assemblies. The large difference in neutron scattering length between hydrogen and deuterium allows contrast variation experiments to be performed and enables H/D isotopic labeling to be used for selective and systematic analysis of the local structure, dynamics, and interactions of multi-component systems. This overview describes the available techniques and summarizes their practical application to the study of biomolecular systems.

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An investigation of the structure of Alfalfa mosaic virus by small-angle neutron scattering

Cited by 44 publications

References 23 publications

Small‐Angle Scattering of X‐Rays and Neutrons

Small‐Angle Scattering of X‐Rays and Neutrons

Structure of clathrin-coated vesicles from small-angle scattering experiments

Neutron Scattering Techniques and Applications in Structural Biology

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