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Figure 7
(a) Part of the 7.2 Å MIR map of T30S in the expected vicinity of protein S15, contoured at a signal-to-noise signal of 0.7 (green) and 1.1σ (magenta) showing features which resemble the structure of this protein as determined by NMR and X-ray crystallography. Two-thirds of the protein's backbone is overlaid on it. Note the fit of most of the main helices, and the missing density around the flexible chain, except for its helical end. The regions coloured red are of a higher density, presumably hosting RNA chains. (b) The area shown in (a) of the 5.5 Å extended map, contoured at 0.85σ level. Note that the areas deficient of density in the 7.2 Å map remain so also after the extension to 5.5 Å. (c) A view of a typical part of the α-helix. Note the perturbations that may indicate side chains, indicated by white arrows, among which one points at a possible side-chains interaction. (d) A cross section through the part of the map shown in (c).

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 6| Part 4| July 1999| Pages 928-941
doi:10.1107/S0909049599006664
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