X-ray small angle scattering with substances of biological interest in diluted solutions

Kratky, O.

doi:10.1016/s0079-6107(63)80015-2

Cited by 309 publications

(102 citation statements)

References 79 publications

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“…Within the experimental error these values are in agreement with those reported from the primary structure analyses of the L18 and L25 proteins, The volumes of the protein molecules were calculated via Porod's invariant (cf. [14] ); the results were 21 700 A a (L18) and 17 400 A a (L25). Although these volumes only should be considered as the very first approximation, it is interesting to note that the prolate ellipsoids of the indicated shapes (figs.…”

Section: Resultsmentioning

confidence: 91%

Small‐angle X‐ray scattering study of the 5S RNA binding proteins L18 and L25 from Escherichia coli ribosomes

Österberg

Sjöberg

1976

FEBS Letters

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Section: Resultsmentioning

confidence: 91%

Small‐angle X‐ray scattering study of the 5S RNA binding proteins L18 and L25 from Escherichia coli ribosomes

Österberg

Sjöberg

1976

FEBS Letters

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“…The relative values of l(O)lc (c = sample concentration) gives relative molecular weights Mr of the proteins as a control of the data [26]. If the structure is sufficiently elongated, the averaged radius of gyration of the cross-sectional structure Rxs and the averaged cross-sectional intensity at zero angle [I(Q).…”

Section: Analysis Of Reduced X-ray and Neutron Datamentioning

confidence: 99%

Factor VIIa and the extracellular domains of human tissue factor form a compact complex: A study by X‐ray and neutron solution scattering

et al. 1995

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The four-domain structure of human factor Vlla and the two-domain structure of tissue factor form a tight complex to initiate blood coagulation. By solution scattering, the mean X-ray and neutron radii of gyration Re (which determine macromolecular elongation) were found to be 3.25 nm, 2.13 nm and 3.14 nm (+ 0.13 rim) for factor VIIa, the extracellular region of tissue factor and their complex in that order. The mean cross-sectional radii of gyration Rxs were 1.33 rim, 0.56 nm and 1.42 nm ( + 0.13 nm) in that order. The mean lengths were 10.3 nm, 7.7 nm and 10.2 nm in that order. The data show that, in solution, the free proteins have extended domain structures, and the complex is formed by a compact side-by-side alignment of the two proteins along their long axes. The high binding affinity of tissue factor for factor Vlla may thus be accounted for by the occurrence of many intermolecular contacts in the complex.

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“…Peter WILHELM, Ingrid PILZ, Andrew N. LANE, and Kasper KIRSCHNER Institut fur Physikalische Chemie der Universitat Graz; and Abteilung fur Biophysikalische Chemie des Biozentrums der Universitat Base1 (Received April 6/July 22,1982) The a and 0 2 subunits of tryptophan synthase were investigated by small-angle X-ray scattering. The molecular parameters are: radius of gyration, CI: 1.95 nm, pz : 3.01 nm; maximum particle diameter, CI: 5.8 nm, p 2 : 10.5 nm; and hydrated volume, CI : 60 nm3, p2 160 nm'.…”

Section: Small-angle X-ray Scattering Studies Of Tryptophan Synthase mentioning

confidence: 99%

Small‐Angle X‐Ray Scattering Studies of Tryptophan Synthase from Escherichia coli and Its α and β₂ Subunits

Wilhelm

Pilz

Lane

et al. 1982

European Journal of Biochemistry

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The a and 0 2 subunits of tryptophan synthase were investigated by small-angle X-ray scattering. The molecular parameters are: radius of gyration, CI: 1.95 nm, pz : 3.01 nm; maximum particle diameter, CI: 5.8 nm, p 2 : 10.5 nm; and hydrated volume, CI : 60 nm3, p2 160 nm'. The shape of the CI subunit can best be described by a circular cylinder, slightly tapered at one end. An elongated elliptical cylinder with its cross section larger in the middle than at the ends was found to be a model equivalent in scattering to the p2 subunit.The CI& enzyme complex was found to have a radius of gyration of 4.01 nm, a maximum length of 13.5 nm, and a hydrated volume of 270 nm3. No satisfactory fit of the scattering data was obtainable by mere apposition of the models of the CI and p 2 subunits. Two cylinders overlapping laterally fit the experimental data considerably better, suggesting changes in the conformation of the subunits on forming the CI& complex.Tryptophan synthase from Escherichia coli is an CI& bienzyme complex, which catalyses the following reactions :Reaction (1) is catalyzed by the CI subunit and 100-fold more efficiently by the (x& complex. Reaction (2) is catalyzed by the fl2 subunit and 50-fold more efficiently by the complex. This mutual activation is thought to arise from heterologous subunit-subunit interactions during assembly of the complex. Moreover, the active sites appear to be juxtaposed at the intersubunit interface [l].The information on the structure and function of the complex and the component subunits has been reviewed recently [I]. Meanwhile the nucleotide sequences of the corresponding genes have been determined for E. roli [2], other enteric bacteria [3], and for Saccharomyces cerevisiae [4], showing that the amino acid sequences of the CI and / 3 polypeptide chains are highly conserved. Further, limited proteolysis has revealed that both the (x subunit ( M , 28727) and the p protomer (M, 42988) are composed of two autonomously folding structural domains that probably form the corresponding active sites at the interdomain interfaces [5 -91. Except for a preliminary crystallographic study of the a subunit [lo] and an estimate of the distance between the two active sites [Ill, little direct evidence on the tertiary and quaternary structure of tryptophan synthase and its subunits is available to date.In this paper we present the results of small-angle X-ray scattering studies on the CI and p2 subunits and the a& complex of tryptophan synthase. The data were fitted to various models equivalent in scattering and support a scheme for the assembly of the complex from its subunits. MATERIALS AND METHODS EnzymesTryptophan synthase (x-& complex was purified from the overproducing strain Escherichia coli trpR trpAEDl02/ F'trpAEDl02 [12]. The excess CI subunit produced by this strain was purified by affinity chromatography [13]. The p 2 subunit was prepared from the pure CI& complex by heat denaturation as described [12,14]. Protein aggregates were removed by gel chromatography on Sephacryl S200 (...

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X-ray small angle scattering with substances of biological interest in diluted solutions

Cited by 309 publications

References 79 publications

Small‐angle X‐ray scattering study of the 5S RNA binding proteins L18 and L25 from Escherichia coli ribosomes

Small‐angle X‐ray scattering study of the 5S RNA binding proteins L18 and L25 from Escherichia coli ribosomes

Factor VIIa and the extracellular domains of human tissue factor form a compact complex: A study by X‐ray and neutron solution scattering

Small‐Angle X‐Ray Scattering Studies of Tryptophan Synthase from Escherichia coli and Its α and β₂ Subunits

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X-ray small angle scattering with substances of biological interest in diluted solutions

Cited by 309 publications

References 79 publications

Small‐angle X‐ray scattering study of the 5S RNA binding proteins L18 and L25 from Escherichia coli ribosomes

Small‐angle X‐ray scattering study of the 5S RNA binding proteins L18 and L25 from Escherichia coli ribosomes

Factor VIIa and the extracellular domains of human tissue factor form a compact complex: A study by X‐ray and neutron solution scattering

Small‐Angle X‐Ray Scattering Studies of Tryptophan Synthase from Escherichia coli and Its α and β2 Subunits

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Small‐Angle X‐Ray Scattering Studies of Tryptophan Synthase from Escherichia coli and Its α and β₂ Subunits