THE IN-SITU STRUCTURE OF RIBOSOMAL-PROTEINS FROM POLARIZED NEUTRON-SCATTERING

Methods of isotopic substitution are widely used in neutron scattering for the determination of the in situ structure of macromolecular comp onents. The contrast created by substitution of the hydrogen isotope H -1 (proton) by H-2 (deuteron) is the most prominent example in contras t variation. A further increase of the contrast is achieved if a polar ized neutron beam is scattered by polarized nuclear spins in the sampl e. This so called spin-contrast-variation method is used to determine the position of the protein L1 in the 50S subunit of the E. coli ribos ome and proteins S6 and S10 in the 70S ribosome.