Small-angle X-ray scattering (SAXS) measurements of proteins in solution are becoming increasingly popular with biochemists and structural biologists owing to the presence of dedicated high-throughput beamlines at synchrotron sources. As part of the ESRF Upgrade program a dedicated instrument for performing SAXS from biological macromolecules in solution (BioSAXS) has been installed at the renovated BM29 location. The optics hutch has been equipped with new optical components of which the two principal elements are a fixed-exit double multilayer monochromator and a 1.1 m-long toroidal mirror. These new dedicated optics give improved beam characteristics (compared with the previous set-up on ID14-3) regarding the energy tunability, flux and focusing at the detector plane leading to reduced parasitic scattering and an extended s-range. User experiments on the beamline have been successfully carried out since June 2012. A description of the new BioSAXS beamline and the set-up characteristics are presented together with examples of obtained data.

The ISPyB information-management system for crystallography has been adapted to include data from small-angle X-ray scattering of macromolecules in solution experiments.

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Associated strangeness production was studied in the pp ! ! p + p reaction at the CERN antiproton facility LEAR using the experimental setup of PS185. Results from two high{statistics measurements at incident a n tiproton momenta of 1:642 and 1.918 GeV/c are reported. Approximately 40 000 reconstructed events at each momentum have allowed us to measure the total and dierential cross-sections, the spin polarizations, the spin correlations, and the singlet fractions of the pair. Since the decays of both the and the w ere simultaneously observed in the same detector, we are able to provide upper limits on CP and CPT violation phenomena in the weak interaction.

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