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

The small angle neutron scattering technique is a valuable method for the characterization of morphology of various materials. It can probe inhomogeneities in the sample (whether occurring naturally or introduced through isotopic substitution) at a length scale from the atomic size (nanometers) to the macroscopic (micrometers) size. This work provides an overview of the small angle neutron scattering facilities at the National Institute of Standards and Technology and a review of the technique as it has been applied to polymer systems, biological macromolecules, ceramic, and metallic materials. Specific examples have been included.

/pdf/small-angle-neutron-scattering-at-the-national-institute-of-clgyee280q.pdf

Small Angle Neutron Scattering at the National Institute of Standards and Technology

▪ Abstract Exciting progress has been made in the last decade by those who use physical methods to study the structure of the ribosome and its components. The structures of 10 ribosomal proteins and three isolated ribosomal protein domains are known, and the conformations of a significant number of rRNA sequences have been determined. Electron microscopists have made major advances in the analysis of images of ribosomes, and microscopically derived ribosome models at resolutions approaching 10A are likely quite soon. Furthermore, ribosome crystallographers are on the verge of phasing the diffraction patterns they have had for several years, and near-atomic resolution models for entire ribosomal subunits could emerge from this source at any time. The literature relevant to these developments is reviewed below.

The three-dimensional structure of the ribosome and its components

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.

Neutron low angle scattering studies of the 50S subunit of E. coli ribosomes with the contrast variation method reveals large fluctuations in the scattering density. A region of relatively low scattering density, rich in proteins, surrounds an RNA-rich core of higher scattering density. The centers of mass of the RNA and protein parts of the 50S subunit are separated by a distance (20 A) that is considerably smaller than that reported in previous studies.

New low resolution model for 50S subunit of Escherichia coli ribosomes.

The label triangulation method and the mixed isomorphous replacement principle

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The label triangulation method and the mixed isomorphous replacement principle