Small Angle Scattering of X-Rays

Escherichia coli sigma 70 and NusA proteins. I. Binding interactions with core RNA polymerase in solution and within the transcription complex.

Positions of S2, S13, S16, S17, S19 and S21 in the 30 S ribosomal subunit of Escherichia coli.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2881%2981076-9

Topography of interaction of Escherichia coli RNA polymerase subunits with lac UV5 promoter

Neutron scattering has been an established technique in solid state physics for some 30 years and in the last 10 years has had a significant impact in biological structure determination. This is especially true in the field of low to medium resolution structure, where complementary techniques are electron microscopy, X-ray scattering and the more indirect biophysical techniques such as hydrodynamic measurements. Small angle neutron scattering from solutions of particles and diffraction from ordered or partially ordered arrays of particles have made it possible to examine the distribution of different components of a biomolecular complex in-situ by substituting D20 for H20 in the molecular environment and/or D for H in the complex. Such investigations cannot be performed with other techniques. Several reviews on applications of neutron scattering have been published in the last few years [e.g. 1, 2, 3].

Low resolution structures of biological complexes studied by neutron scattering.

In all organisms the multi-subunit enzyme DNA-dependent RNA polymerase catalyses the first basic step in gene expression, the transcription of DNA into RNA. The neutron small-angle scattering effects were studied in the Guinier region by applying the contrast-matching technique. Isotopic labelling was realised by culturing fully deuterated E. coli cells in a heavy-water medium containing deuterated substrates. One or two completely deuterated components (subunits) of polymerase holoenzyme (composition formula α2ββ′σ, molecular weight 497000) were recombined with the remaining natural (`hydrogenated') subunits for these neutron measurements. Measurements are presented of radii of gyration R, overall shapes, and pair distances d, of three components (subunits α2β,β′) in RNA polymerase of E. coli. The subunits β′, β and α2 are obviously rather elongated in situ and exhibit (as scattering-equivalent prolate ellipsoids) axial ratios of about 7:1 up to 9:1. The intersubunit centre of gravity distances were analysed to be 7.3 ± 0.8 nm for β−β′, 8.2 ± 1.2 nm for α2−β′ and 7.0 ± 1.7 nm for α2−β.

Determination of intersubunit distances and subunit shape parameters in DNA‐dependent RNA polymerase by neutron small‐angle scattering

In the E. coli 50 S ribosomal subunit, proteins L7/L12 and L10 were deuterated by partial reconstitution. The distance between L7/L12 and L10 was measured by the label triangulation method and was found to be approximately 100 A or, with low probability, 60 to 70 A, depending on the concentration.

Neutron scattering measurements with the label triangulation method on the 50 S subunit of E. coli ribosomes.

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Determination of intersubunit distances and subunit shape parameters in DNA‐dependent RNA polymerase by neutron small‐angle scattering

Neutron scattering measurements with the label triangulation method on the 50 S subunit of E. coli ribosomes.