The protein L2 is found in all ribosomes and is one of the best conserved proteins of this mega-dalton complex. The protein was localized within both the isolated 50 S subunit and the 70 S ribosome of the Escherichia coli bacteria with the neutron-scattering technique of spin-contrast variation. L2 is elongated, exposing one end of the protein to the surface of the intersubunit interface of the 50 S subunit. The protein changes its conformation slightly when the 50 S subunit reassociates with the 30 S subunit to form a 70 S ribosome, becoming more elongated and moving approximately 30 A into the 50 S matrix. The results support a recent observation that L2 is essential for the association of the ribosomal subunits and might participate in the binding and translocation of the tRNAs.

Mapping of protein positions in the ribosomal subunits was first achieved for the 30S subunit by means of neutron scattering about 15 years ago. Since the 50S subunit is almost twice as large as the 30S subunit and consists of more proteins, it was difficult to apply classical contrast variation techniques for the localisation of the proteins. Polarisation dependent neutron scattering (spin-contrast variation) helped to overcome this restriction. Here a map of 14 proteins within the 50S subunit from Escherichia coli ribosomes is presented including the proteins L17 and L20 that are not present in archeal ribosomes. The results are compared with the recent crystallographic map of the 50S subunit from the archea Haloarcula marismortui.

A muon beam polarimeter was built for the SMC experiment at the CERN SPS, for beam energies of 100 and 190 GeV. The beam polarisation is determined from the asymmetry in the elastic scattering off the polarised electrons of a ferromagnetic target whose magnetisation is periodically reversed. At muon energies of 100 and 190 GeV the measured polarisation is Pμ=−0.80±0.03 (stat.)±0.02 (syst.) and Pμ=−0.797±0.011 (stat.)±0.012 (syst.), respectively. These results agree with measurements of the beam polarisation using a shape analysis of the decay positron energy spectrum.

Polarized neutron scattering from dynamically polarized nuclear spin targets has become a method of macromolecular structure research. The contrast created by substitution of the hydrogen isotope H-1 by H-2 is increased by almost a factor of three if polarized neutrons are scattered by polarized nuclear spins in the sample (spin contrast variation). Therefore, this method is also suitable to determine small or weakly contrasted labels. Proteins with a mass less than 1 wt.% of the background particle were localized. In this paper, an extension of our structural model for the 50S subunit by the in situ structure determination of the protein L14 is presented.

Arrays of limited streamer tubes of the Iarocci type were deployed in our experiment at CERN as part of a forward muon detector system with provisions for the beam to pass through the center of each panel in the array. A total of 16 4 m×4 m panels were assembled with inductive readout strips on both sides of each panel. An active feedback system was deployed to regulate the high voltage to the streamer tubes to insure a constant efficiency for minimum ionizing particles. The arrays were operated in this environment for over five years of data taking. Streamer tube track-reconstruction efficiencies and tube replacement rates are reported.

The polarized target of the Spin Muon Collaboration at CERN was used for deep inelastic muon scattering experiments during 1993–1996 with a polarized muon beam to investigate the spin structure of the nucleon. Most of the experiments were carried out with longitudinal target polarization and 190 GeV muons, and some were done with transverse polarization and 100 GeV muons. Protons as well as deuterons were polarized by dynamic nuclear polarization (DNP) in three kinds of solid materials — butanol, ammonia, and deuterated butanol — with maximum degrees of polarization of 94%, 91% and 60%, respectively. Considerable attention was paid to the accuracies of the NMR polarization measurements and their analyses, the accuracies achieved were between 2.0% and 3.2%. The SMC target system with two cells of opposite polarizations, each cell 65 cm long and 5 cm in diameter, constitutes the largest polarized target system ever built and facilitates accurate spin asymmetry measurements. The design considerations, construction and performance of the target are reviewed.

The 1996 data taking of the SMC experiment used polarized protons to measure the spin-dependent structure function g(1) of the proton. Three liters of solid granular ammonia were irradiated at the Bonn electron linac in order to create the paramagnetic radicals which are needed for polarizing the protons. Proton polarizations of +/- (90 +/- 2.5)% were routinely reached. An analysis based on a theoretical line shape for spin-1. systems with large quadrupolar broadening was developed which allowed the nitrogen polarization in the ammonia to be determined with a 10% relative error. The measured quadrupolar coupling constant of N-14 agrees well with earlier extrapolated values. The polarization of the nitrogen nuclei was measured as a function of the proton polarization in order to provide a test of the equal spin temperature (EST) hypothesis. It was found to be closely valid under the dynamic nuclear polarization conditions with which the protons are polarized. Large deviations from EST could be induced by cross relaxing the proton and nitrogen spin systems at low fields. Nitrogen polarizations up to 40% were reached by these means. (C) 1998 Elsevier Science B.V. All rights reserved.

We present the final results of the spin asymmetries A(1) and the spin structure functions g(1) of the proton and the deuteron in the kinematic range 0.0008 < x < 0.7 and 0.2 < Q(2) < 100 GeV2. For the determination of A(1), in addition to the usual method which employs inclusive scattering events and includes a large radiative background at low x, we use a new method which minimizes the radiative background by selecting events with at least one hadron as well as a muon in the final state. We find that this hadron method gives smaller errors for x < 0.02, so it is combined with the usual method to provide the optimal set of results. [S0556-2821(98)07017-9].

We present a next-to-leading order QCD analysis of the presently available data on the spin structure function g(1) including the final data from the Spin Muon Collaboration. We present results for the first moments of the proton, deuteron, and neutron structure functions, and determine singlet and nonsinglet parton distributions in two factorization schemes. We also test the Bjorken sum rule and find agreement with the theoretical prediction at the level of 10%. [S0556-2821(98)07117-3].

Polarized neutron scattering from dynamically polarized nuclear spin targets has become a method of macromolecular structure research. The contrast created by substitution of the hydrogen isotope 1H by 2H is increased by almost a factor of three if polarized neutrons are scattered by polarized nuclear spins in the sample (spin contrast variation). Therefore, this method is also suitable to determine small or weakly contrasted labels. Proteins with a mass less than 1 wt% of the background particle were localized. In this paper, the extended version of protein localization is presented: proteins L1, L2, L3, L4 in 50 S and proteins S6, S10 in 70 S. Furthermore, even the position of two weakly contrasted tRNAs bound at the elongating 70 S ribosome were determined.