ID15A is a newly refurbished beamline at the ESRF devoted to operando and time‐resolved diffraction and imaging, total scattering and diffraction computed tomography. The beamline is optimized for rapid alternation between the different techniques during a single operando experiment in order to collect complementary data on working systems. The high available energy (up to 120 keV) means that even bulky and highly absorbing systems may be studied. The beamline is equipped with optimized focusing optics and a photon‐counting CdTe pixel detector, allowing for both unprecedented data quality at high energy and for very rapid triggered experiments. A large choice of imaging detectors and ancillary probes and sample environments is also available.
small variability to cover Se and Br edges). The 24ID-E beamline is equipped with a MD2 microdiffractometer, which is used to provide stable and well collimated beam from 5 to 100 microns in diameter and capable of visualizing micron-sized crystals. These operational beamlines are currently open to general APS users. Installation of a bending magnet beamline is now in progress and expected to be completed by the end of this year. NE-CAT is a consortium of scientists organized to design, construct and operate a structural biology sector at the APS. This facility will be used to focus on NE-CAT research on structural studies involving technically challenging crystallographic projects. In order to meet these needs, an ALS robot for screening a large number of crystals is now being commissioned, a microfocus diffractometer MD-2 is installed on 24ID-E beamline and several novel hardware and software ideas will be implemented.
PROXIMA 2A is a new micro-focus and energy tunable beamline dedicated to biological macromolecular crystallography at Synchrotron SOLEIL. The beamline officially opened in March 2013, and its first year of user operation has yielded excellent results. The X-ray source is a powerful in-vacuum U24 undulator coupled to a cryo-cooled Si[111] channel-cut monochromator and a pair of focussing bimorph mirrors in Kirpatrick-Baez configuration. This combination delivers a photon flux of over 10**12 ph/s into a focal spot of 10 μm × 5 μm (H×V FWHM), which is tunable over 6 – 15 keV. The supports of the optical elements have been designed to minimise the effects of vibrations and thermal dilations on the X-ray beam position, which is stable to within 5 microns over a day. The experimental station consists of a high performance micro-diffractometer, a cryostream, an area detector (ADSC Q315r), and an X-ray fluorescence detector. The X-ray energies for MAD experiments are directly calibrated on the sample. A robot equipped with a large 9 uni-puck dewar (CATS Irelec) is available to users for the automated transfer and screening of cryo-cooled samples. The users launch their experiments via an MXCuBE interface [1], which permits the centering of the sample, collecting of diffraction images, recording of X-ray spectra and the transfer of samples. The X-ray diffraction data are of an excellent quality, and the users readily exploit the micro-focused X-rays to select the best zones of their crystals. The first year of results from users has yielded a variety of success stories including novel protein structures resolved from crystals as small as 5 microns, as well as those solved by SAD & MAD methods. The future perspectives include automated helical and grid scans, in situ plate screening and multi-crystal merging techniques.
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