Synchrotron radiation and structural biology

The motivation for this Special Issue has arisen from the award of the Nobel Prize in Chemistry (shared) in 1997 to Sir John Walker of the MRC's Laboratory of Molecular Biology [see J. Synchrotron Rad. (1998). 5, 1323]. This included the structure elucidation of the enzyme F1ATPase, which included extensive data collection at the SRS in Daresbury (Abrahams et al., 1994). This is then a chance to salute that work in the pages of this journal. A photograph of Sir John Walker's prize-winning team (Fig. 1) and a schematic representation of the structure of F1-ATPase (Fig. 2) are shown. This is a further signal of the importance of synchrotron radiation in structural biology, which is seeing considerable growth. A range of techniques using synchrotron radiation are contributing: speci®cally protein crystallography, ®bre diffraction, XAFS, small-angle scattering and microscopy. Other techniques are also growing in importance in the UV/VUV region of the spectrum. These include circular dichroism and time-resolved uorescence utilizing the single-bunch mode of the synchrotron radiation operation. In this special issue the Editorial Board of the Journal of Synchrotron Radiation (JSR) has commissioned various articles as a sample of the various aspects of synchrotronradiation-based structural biology. We are very grateful to all the authors for their articles. These have been fully refereed in the usual way. Also we are fortunate to have an overview article by Tom Blundell and Louise Johnson, who wrote one of the most popular monographs (Blundell & 809