Following the long shutdown needed for the preparation and construction work required for Phase I of the ESRF Upgrade Programme, user service at the ESRF’s structural biology facilities was restored in May. Following a week or two of frenetic activity, the beamlines were ready and operational as planned.

Despite the relatively short year of operation, 2012 has been a busy year with much activity devoted to the construction of new beamlines and the deployment of new equipment. The ESRF’s BioSAXS facility has been re-opened, with a completely new optical configuration, at the refurbished beamline BM29. The use of a high-bandpass multilayer monochromator system combined with new focusing optics means a smaller focal spot and increased flux. This, coupled with energy tunability, allows for greater flexibility in the experiments that can be performed. Moreover, while maintaining the operation of the automated liquid sample handler, we have extended the range of options available at BM29 by including an HPLC system for the study of proteins and protein complexes “straight off the column”. SAXS experiments at BM29 now also benefit from an advanced beamline control GUI and automatic data processing via software developed at EMBL Hamburg. We have also extended the functionality of our crystallography database ISPyB with enhancements specifically designed for bioSAXS measurements.

The newest of our macromolecular crystallography beamlines, ID30A, continues to make good progress. Optics and experimental hutches have been constructed and the commissioning of the X-ray optics has begun. Initial results are promising with all components conforming to expectations. X-rays have also been successfully delivered to the experimental hutches - a major milestone en route to user operation. The automation of sample handling has been a key success of the ESRF Structural Biology Group for more than a decade. ID30A will extend this capability, bringing new opportunities for structural biology. Automatic sample changing will remain a core element of beamline operation and will be enhanced by the availability of high capacity sample dewars and faster, more robust robots. In the longer term, and to further increase capacity, it will be necessary to update the sample holder itself. Work is underway to provide a new sample holder that is compatible with present standards but which will allow higher precision mounting and greater reliability. This development is being undertaken in cooperation with our colleagues at other synchrotron sites and with the appropriate user communities.

The work presented in this highlights chapter represents only a very small fraction of the science reported by the ESRF’s structural biology user community. Nevertheless, even a brief perusal of the articles presented here makes it clear that we continue to facilitate extremely high-quality research over a broad range of topics of fundamental biological interest. As usual, the space available means that we limit ourselves to highlighting some general themes and have not been able to include a very large number of deserving cases. Approximately 30% of the articles presented in the chapter concern the crystal structures of membrane proteins, illustrating the continuing importance of this research area throughout Europe. Today, however, we are seeing more sophisticated sets of experiments that provide an understanding, at an atomic level, of how these crucial cellular components function. We are proud, as a group, to have helped in a small way with the work that lead to the award for the 2012 Nobel Prize in Chemistry.

By the time next year’s ESRF Highlights appears we expect the first components of the ID30A complex to be in user operation. These will be a beamline (ID30A1) for the completely automatic analysis of the diffraction properties of protein crystals and the second of our dedicated microfocus beamlines for MX (ID30A3). However, this will not be the end of our efforts to continue to produce world leading instruments for MX and ideas are under discussion to further enhance, or even revolutionise, the practice of structural biology at synchrotron sources. These ideas may crystallise in the coming year and will form part of Phase II of the ESRF Upgrade Programme.


S. McSweeney and G. Leonard