ABSTRACT
The North West Structural Genomics Centre's beamline, MAD10, at the SRS receives the central part of the radiation fan (0.5 mrad vertically, 4 mrad horizontally) produced by a new 2.46 T ten-pole wiggler. The optical arrangement of the beamline consists of a Rh-coated collimating Si mirror, a fixed-exit-beam double-crystal monochromator with sagittal bending for horizontal focusing and a second Rh-coated Si mirror for vertical focusing. The double-crystal Si (111) monochromator allows data collection in the 5-13.5 keV photon energy range with rapid (subsecond) tunability and high energy resolution. The monochromatic beam is optimized through a 200 microm collimator. The beamline end station has been designed around a Mar desktop beamline with high-throughput cryogenic sample changer, Mar225 CCD detector, liquid-N(2) autofill system and an ORTEC C-TRAIN-04 energy-resolving high-count-rate X-ray fluorescence detector. The instrument is optimized for MAD/SAD applications in protein crystallography with the additional mode of operation of online single-crystal EXAFS studies on the same crystals. Thus, screening of metals/Se in the crystal can be performed quickly prior to MAD/SAD data collection by exciting the crystal with X-rays of appropriate energy and recording an energy-dispersive fluorescence spectrum. In addition, this experimental set-up allows for parallel XAFS measurements on the same crystal to monitor 'radiation-induced' changes, if any, in e.g. the redox state of metal centres to be detected for a 'metallic' functional group during crystallographic data collection. Moreover, careful minimization of the thickness of the Be window maximizes the intensity performance for the 2.0-2.5 A softer wavelength range. This range also covers the K-edges of a number of important 3d transition metals as well as the L-edges of xenon and iodine and enhanced sulfur f ''.
