Abstract
ID14-4 at the ESRF is the first tunable undulator-based macromolecular crystallography beamline that can celebrate a decade of user service. During this time ID14-4 has not only been instrumental in the determination of the structures of biologically important molecules but has also contributed significantly to the development of various instruments, novel data collection schemes and pioneering radiation damage studies on biological samples. Here, the evolution of ID14-4 over the last decade is presented, and some of the major improvements that were carried out in order to maintain its status as one of the most productive macromolecular crystallography beamlines are highlighted. The experimental hutch has been upgraded to accommodate a high-precision diffractometer, a sample changer and a large CCD detector. More recently, the optical hutch has been refurbished in order to improve the X-ray beam quality on ID14-4 and to incorporate the most modern and robust optical elements used at other ESRF beamlines. These new optical elements will be described and their effect on beam stability discussed. These studies may be useful in the design, construction and maintenance of future X-ray beamlines for macromolecular crystallography and indeed other applications, such as those planned for the ESRF upgrade.
Highlights
ID14-4 was commissioned in 1998 and has been instrumental in the determination of the structures of many biologically important structures, including the 30S ribosomal subunit (Wimberly et al, 2000), tubulin (Ravelli et al, 2004) and the complement component C3 (Janssen et al, 2005), as well as making a significant contribution to structural studies on the 70S ribosome (Selmer et al, 2006)
ID14-4 was commissioned with a fixed-exit Kohzu double-crystal monochromator (DCM) for energy selection and a toroidal mirror to focus the X-ray beam
Later experience gained from the operation of other macromolecular crystallography (MX) beamlines at the ESRF has shown that the channel-cut monochromators of both ID23-1 (Nurizzo et al, 2006) and
Summary
ID14-4 was commissioned in 1998 and has been instrumental in the determination of the structures of many biologically important structures, including the 30S ribosomal subunit (Wimberly et al, 2000), tubulin (Ravelli et al, 2004) and the complement component C3 (Janssen et al, 2005), as well as making a significant contribution to structural studies on the 70S ribosome (Selmer et al, 2006). ID14-4 was commissioned with a fixed-exit Kohzu double-crystal monochromator (DCM) for energy selection and a toroidal mirror to focus the X-ray beam. Later experience gained from the operation of other macromolecular crystallography (MX) beamlines at the ESRF has shown that the channel-cut monochromators of both ID23-1 (Nurizzo et al, 2006) and. It was decided to replace the original mirror and vessel with a set-up similar to ID23-1 This upgrade of the optical components complements an earlier refurbishment of the experimental hutch. These improvements, when combined with the continued improvement of automation protocols (Beteva et al, 2006), allow standard X-ray diffraction experiments, including multiple anomalous diffraction (MAD), to be and robustly performed. We describe in detail a decade of systematic improvements on ID14-4 that will be beneficial to the construction of other synchrotron radiation beamlines
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