Experimental and theoretical large‐angle X‐ray diffuse scattering by globins in solution. Sensitivity of the method

Fedorov, B.A.; Kröber, R.; Damaschun, G.; Ruckpaul, K

doi:10.1016/0014-5793(76)80628-x

Cited by 6 publications

(3 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The scattering curve calculation was made by the 'cube method' [3,4] taking into account solvent influence. The method was modified to take into consideration more exactly cavities and clefts in a protein molecule accessible to the solvent.…”

Section: Resultsmentioning

confidence: 99%

The structure of ribonuclease in solution does not differ from its crystalline structure

et al. 1978

Self Cite

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 99%

The structure of ribonuclease in solution does not differ from its crystalline structure

et al. 1978

Self Cite

View full text Add to dashboard Cite

“…X-ray scattering is fundamentally rooted in orientationally averaged atomic scattering. By basing the analysis of macromolecular high angle scattering on atomic scattering ( − ), and by including the effects of thermal factors ( , ), high angle scattering becomes a direct measure of structural change that can be quantitatively related to structural models. In particular, we have found that the shapes of difference high angle scattering patterns calculated from models of oxidation-dependent conformational change in cytochrome c are distinguishable, and depend on both the sites and magnitudes of structural change.…”

Section: Discussionmentioning

confidence: 99%

“…The availability of high-flux, third generation synchrotron X-ray sources and the development of large area solid-state detectors have opened up new opportunities for collecting high-precision, high-angle X-ray scattering patterns for proteins in solution (27). The opportunity to detect highangle scattering is significant since it probes distance correlations on length scales that are small compared to the macromolecular dimensions, and potentially contains information on the details of protein structure in solution (28,29). Methods have been developed for accurately calculating scattering patterns for proteins based on atomic coordinates (30).…”

mentioning

confidence: 99%

Protein Conformations Explored by Difference High-Angle Solution X-ray Scattering: Oxidation State and Temperature Dependent Changes in Cytochrome C

2002

View full text Add to dashboard Cite

We demonstrate the use of high-angle X-ray scattering to explore protein conformational states in solution by resolving oxidation state- and temperature-dependent changes in the conformation of horse heart cytochrome c. Several detailed models exist for oxidation-dependent changes in mitochondrial class I c cytochromes determined by X-ray crystallography and solution NMR techniques. These models differ in the magnitude and locations of structural change. Our scattering measurements show that high-angle X-ray scattering can discriminate between these models, and that the experimental scattering data for horse cytochrome c can be best reconciled with selected NMR models for the same protein. These results demonstrate the ability to use high-angle X-ray scattering to resolve conformational states of proteins in solution, and to relate these measurements to detailed structural models. Furthermore, temperature-dependent changes are found in the high angle scattering patterns for horse cytochrome c, illustrating the sensitivity of these measurements to dynamic aspects of protein structure. These results demonstrate the ability to use difference high angle scattering as a quantitative monitor of reaction-linked changes in protein conformation and structural dynamics. Synchrotron-based high-angle scattering holds promise as a widely applicable, high throughput technique for exploring conformational states linked to physiological protein function, for resolving configurational differences between protein structures in solution and crystalline states, and for bridging the gap between solution NMR and crystallographic structure techniques.

show abstract

Comparison of the structure of ribosomal 5S RNA from E. coli and from rat liver using X-ray scattering and dynamic light scattering

Jj¹,

Zirwer³

et al. 1986

Eur Biophys J

View full text Add to dashboard Cite

The structure of eukaryotic ribosomal 5S RNA from rat liver and of prokaryotic 5S RNA from E. coli (A-conformer) have been investigated by scattering methods. For both molecules, a molar mass of 44,500 +/- 4,000 was determined from small angle X-ray scattering as well as from dynamic light scattering. The shape parameters of the two rRNAs, volume Vc, surface Oc, radius of gyration Rs, maximum dimension of the molecule L, thickness D, and cross section radius of gyration Rsq, agree within the experimental error limits. The mean values are Vc = 57 +/- 3 nm3, Oc = 165 +/- 10 nm2, Rs = 3.37 +/- 0.05 nm, L = 10.8 +/- 0.7 nm, D = 1.57 +/- 0.07 nm, Rsq = 0.92 +/- 0.01 nm. Identical structures for the E. coli 5S rRNA and the rat liver 5S rRNA at a resolution of 1 nm can be deduced from this agreement and from the comparison of experimental X-ray scattering curves and of experimental electron distance distribution functions. The flat shape model derived for prokaryotic and eukaryotic 5S rRNA shows a compact region and two protruding arms. Double helical stems are eleven-fold helices with a mean base pair distance of 0.28 nm. Combining the shape information obtained from X-ray scattering with the information about the frictional behaviour of the molecules, deduced from the diffusion coefficients D020, w = (5.9 +/- 0.2) X 10(-7) cm2 s-1 and (6.2 +/- 0.2) X 10(-7) cm2 s-1 for rat liver 5S rRNA and E. coli 5S rRNA, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

Experimental and theoretical large‐angle X‐ray diffuse scattering by globins in solution. Sensitivity of the method

Cited by 6 publications

References 6 publications

The structure of ribonuclease in solution does not differ from its crystalline structure

The structure of ribonuclease in solution does not differ from its crystalline structure

Protein Conformations Explored by Difference High-Angle Solution X-ray Scattering: Oxidation State and Temperature Dependent Changes in Cytochrome C

Comparison of the structure of ribosomal 5S RNA from E. coli and from rat liver using X-ray scattering and dynamic light scattering

Contact Info

Product

Resources

About