Ion flows and heating at a contracting polar-cap boundary

Data recorded by the POLAR experiment run on the EISCAT radar during the international GISMOS campaign of 3–5 June 1987 are studied in detail. The polar-cap boundary, as denned by an almost shear East-West convection reversal, was observed to jump southward across the EISCAT field of view in two steps at 02:00 and 03:00 Magnetic Local Time and subsequently to contract back between 04:00 and 07:00 M.L.T. An annulus of enhanced ion temperature and non-thermal plasma was observed immediately equatorward of the contracting boundary due to the lag in the response of the neutral-wind pattern to the change in ion flows. The ion flow at the boundary is shown to be relatively smooth at 15 s resolution and directed northward, with velocities which exceed that of the boundary itself. The effect of velocity shears on the beamswinging technique used to derive the ion flows is analyzed in detail and it is shown that, for certain orientations of the cap boundary, spurious flows into the cap can be generated. However, these are much smaller than the observed flows into the polar cap and cannot explain the potential difference across the observed segment of the cap boundary (extending over 2 h of M.L.T.) which is roughly 7 kV. Similarly, an observed slowing of the zonal flow near the boundary cannot be explained as an error introduced by the use of the beamswinging technique. The results could be interpreted as being due to reconnection occurring on the dawn flank of the magnetopause (mapping to the polar cap at 04:30 06:30 M.L.T.). However, they are more consistent with recent observations of slow anti-sunward flow of closed field lines on the flanks of the geomagnetic tail, which appears to be generated by some form of “viscous” coupling to the magnetosheath plasma.

Guanine specific binding at a DNA junction formed by d[CG(5-BrU)ACG]2 with a topoisomerase poison in the presence of Co2+Ions†,‡

The structure of the duplex d[CG(5-BrU)ACG]2 bound to 9-bromophenazine-4-carboxamide has been solved through MAD phasing at 2.0 Å resolution. It shows an unexpected and previously unreported intercalation cavity stabilized by the drug and novel binding modes of Co2+ ions at certain guanine N7 sites. For the intercalation cavity the terminal cytosine is rotated to pair with the guanine of a symmetry-related duplex to create a pseudo-Holliday junction geometry, with two such cavities linked through the minor groove interactions of the N2/N3 guanine sites at an angle of 40°, creating a quadruplex-like structure. The mode of binding of the drug is shown to be disordered, with the major conformations showing the side chain bound to the N7 position of adjacent guanines. The other end of the duplex exhibits a terminal base fraying in the presence of Co2+ ions linking symmetry-related guanines, causing the helices to intertwine through the minor groove. The stabilization of the structure by the intercalating drug shows that this class of compound may bind to DNA junctions as well as duplex DNA or to strand-nicked DNA (‘hemi-intercalated'), as in the cleavable complex. This suggests a structural basis for the dual poisoning of topoisomerase I and II enzymes by this family of drugs.

Determination by MAD-DM of the structure of the DNA duplex d[ACGTACG(5-BrU)]2 at 1.46 Å and 100 K

A four-wavelength MAD experiment on a new brominated octanucleotide is reported here. d[ACGTACG(5-BrU)], C77H81BrN30O32P7, (DNA) = 2235, tetragonal, P43212 (No. 96), a = 43.597, c = 26.268 Å, V = 49927.5 Å3, Z = 8, T = 100 K, R = 10.91% for 4312 reflections between 15.0 and 1.46 Å resolution. The self-complementary brominated octanucleotide d[ACGTACG(5-BrU)]2 has been crystallized and data measured to 1.45 Å at both 293 K and a second crystal flash frozen at 100 K. The latter data collection was carried out to the same resolution at the four wavelengths 0.9344, 0.9216, 0.9208 and 0.9003 Å, around the Br K edge at 0.92 Å and the structure determined from a map derived from a MAD data analysis using pseudo-MIR methodology, as implemented in the program MLPHARE. This is one of the first successful MAD phasing experiments carried out at Sincrotrone Elettra in Trieste, Italy. The structure was refined using the data measured at 0.9003 Å, anisotropic temperature factors and the restrained least-squares refinement implemented in the program SHELX96, and the helical parameters are compared with those previously determined for the isomorphous d(ACGTACGT)2 analogue. The asymmetric unit consists of a single strand of octamer with 96 water molecules. No countercations were located. The A-DNA helix geometry obtained has been analysed using the CURVES program.