Recent advances and applications of diffuse X-ray small-angle scattering on biopolymers in dilute solutions

Kratky, O.; Pilz, Ingrid

doi:10.1017/s0033583500001049

Cited by 94 publications

(32 citation statements)

References 75 publications

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“…(Kratky and Kratky, 1964;Leopold, 1965) combined with the X-ray measuring equipment of Philips allowed automatic operation. The scattered intensities were measured at 65 different scattering angles in a range between 0.002 1 and 0.1 radian; an entrance slit of 120 pm was used.…”

Section: Methodsmentioning

confidence: 99%

“…The equations used for these calculations have already been given in this journal . Summarizing papers about these methods are those of Kratky (1963), Kratky and Pilz (1972), and Pilz (1973). Up to now only the unsmoothed experimentally obtained scattering data are given, because they show clearly the er- __ _________ a c is the concentration of the fragments in solution rors of measurement and the fact that changes in the conformation of the fragments upon the binding of hapten, if any, cause no change in the R value within these errors of measurement (compare Figure 3 and Table I).…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Shape and volume of fragments Fab' and (Fab')2 of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as determined by small-angle x-ray scattering

Pilz¹,

Kratky²,

Licht³

et al. 1975

Biochemistry

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The conformation of two fragments derived from anti-poly(D-alanyl) antibodies, the divalent fragment (Fab')2 and the monovalent fragment Fab', was studied by small-angle X-ray scattering before and after interaction with the tetra-D-alanine amide hapten. More than 90% of the combining sites were occupied by the hapten. No significant changes were observed in the volume or in the radius of gyration, with either of the fragments. This contrasts with the significant decrease in these two parameters found upon reacting the hapten with intact anti-poly(D-alanyl) antibodies (I. Pilz, O. Kratky, A. Licht, and M. Sela (1973), Biochemistry 12, 4998). For Fab', the radius of the whole particle was found to be 3.48 nm in the absence of the hapten and 3.46 nm in its presence, the radius of gyration of the cross-section was 1.37 nm without hapten and 1.38 nm in its presence, and the volume of the particle was 98 nm3 in the absence of the hapten and 91 nm3 in its presence. For (Fab')2 the respective values were 5.06 and 5.05, 1.38 and 1.37, and 182 and 182. These results suggest that a conformational change occurs within the antibody molecule, but not within its Fab fragment, upon reaction with the tetraalanine hapten.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Shape and volume of fragments Fab' and (Fab')2 of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as determined by small-angle x-ray scattering

Pilz¹,

Kratky²,

Licht³

et al. 1975

Biochemistry

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“…This periodicity gives rise to a maximum in the scattering profile, the position of which (Qmax) yields the long period (d-27r/Qm~x), which is controlled by the molecular weight, annealing conditions etc. Kratky and coworkers (Kratky, 1963(Kratky, , 1964Kratky, Pilz & Schmitz, 1966) have performed detailed calibrations of one such polyethylene (Lupolen, Fig. 1 slit systems.…”

Section: Wavelength Smearing Effects In Saxsmentioning

confidence: 99%

Instrumental resolution effects in small-angle scattering

Wignall¹

1991

J Appl Cryst

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Experimentally measured scattering data differ from theoretical curves because of departures from point geometry in a real instrument. In a small‐angle scattering instrument there are three contributions to the smearing of an ideal curve: (1) the angular divergence of the beam; (2) the finite resolution of the detector; and (3) the polychromatic nature of the beam. In general, instrumental‐resolution (smearing) effects are smaller for small‐angle neutron scattering (SANS) than for small‐angle X‐ray scattering (SAXS). This is because most SANS experiments are performed in point geometry (with pinhole collimation) whereas a significant proportion of X‐ray experiments have used long‐slit sources where smearing effects are much larger, particularly at small angles. Hence, corrections to the measured curve are often applied in SAXS experiments to compensate for angular smearing. Less attention has been given to the effects of wavelength smearing in SAXS which is often assumed to be negligible. Similarly, SANS data are routinely analyzed without reference to instrumental smearing effects. The circumstances under which the above assumptions break down are illustrated by a range of experiments comparing data taken from the same samples, run on different types of SAXS and SANS facilities. These experiments indicate some circumstances under which the above effects cannot be neglected.

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“…The use of standards, lupolen in X-ray scattering (Kratky & Pilz, 1972) or water in neutron scattering (Stuhrmann et at., 1976a, b), is recommended, once the absolute scale has been established. The incident flux J'~P can be measured after appropriate attenuation.…”

Section: Iii2 Zero-angle Scattering -Molecular Weightmentioning

confidence: 99%

Small-angle scattering of biological structures

Stuhrmann¹,

Miller²

1978

J Appl Cryst

207

143

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Small‐angle scattering studies on biological structures provide low‐resolution models. More detailed models need a more elaborate analysis in order to show their uniqueness. The representation of small‐angle scattering of both in Cartesian coordinates and polar coordinates is discussed. The degree of non‐uniqueness of structural analysis is best presented in terms of a multipole expansion. Contrast variation leads to the evaluation of the basic scattering functions Jc(κ), Jcs(κ) and Js(κ), which add useful constraints to a model. The experimental aspects of this method in both X‐ray and neutron scattering are discussed. Furthermore, isomorphous (or isotopic) replacement of parts of macromolecular structures have been very useful in structure determination of ribosomes. Kinetic investigations of solutions in the subsecond region have been performed so far only for the investigation of H–D exchange with some proteins. Small‐angle scattering from fibrous and lamellar systems received a considerable impact from a combined use of X‐ray and neutron scattering, as is shown for collagen. Structural changes during active muscle contraction have been investigated both with classical X‐ray equipment and with synchrotron radiation.

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Recent advances and applications of diffuse X-ray small-angle scattering on biopolymers in dilute solutions

Cited by 94 publications

References 75 publications

Shape and volume of fragments Fab' and (Fab')2 of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as determined by small-angle x-ray scattering

Shape and volume of fragments Fab' and (Fab')2 of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as determined by small-angle x-ray scattering

Instrumental resolution effects in small-angle scattering

Small-angle scattering of biological structures

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