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.

ID29 is an ESRF undulator beamline with a routinely accessible energy range of between 20.0 keV and 6.0 keV (= 0.62 Å to 2.07 Å) dedicated to the use of anomalous dispersion techniques in macromolecular crystallography. Since the beamline was first commissioned in 2001, ID29 has, in order to provide an improved service to both its academic and proprietary users, been the subject of almost continuous upgrade and refurbishment. It is now also the home to the ESRF Cryobench facility, ID29S. Here, the current status of the beamline is described and plans for its future are briefly outlined.

MASSIF-1 (ID30A-1) is a new beamline dedicated to the completely automatic characterization and data collection from crystals of biological macromolecules.

The use of third-generation synchrotron sources has led to renewed interest in the effect that ionizing radiation has on crystalline biological materials. Simple criteria have been sought to study the effects systematically. The unit-cell volume of protein crystals shows a linear increase with absorbed dose and has therefore been proposed to be such a measure. This paper demonstrates that the increase is sample dependent, and thus it might not be a useful indicator when comparing different samples. For individual samples, however, the increase can be used to quantify ambient temperature and dose-rate effects. In this study, highly absorbing cubic crystals of holoferritin have been used to accurately determine how cell volume changes with absorbed dose. The experiments show that, for this protein, a dose-rate effect exists and that trapped radicals can be mobilized at ca 180 K.

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