The ID23-1 structural biology beamline at the ESRF

Nurizzo, Didier; Mairs, Trevor; Guijarro, Matias; Rey, Vicente; Meyer, Jens; Fajardo, P.; Chavanne, J.; Biasci, Jean Claude; McSweeney, Seán; Mitchell, Edward P.

doi:10.1107/s0909049506004341

Cited by 157 publications

(140 citation statements)

References 21 publications

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“…The ID23 X-ray source has been described previously (Nurizzo et al, 2006) and is a canted undulator system made up of two undulators with an angular separation of 1.5 mrad. The choice of a 1.5 mrad separation was governed by the need to separate the two beams sufficiently to pass through two distinct diamond front-end windows on one hand and the necessity to minimize the design effort involved in modifying the front-end on the other.…”

Section: The Id23 X-ray Sourcementioning

confidence: 99%

“…Beamlines such as ID23-1 (Nurizzo et al, 2006) and ID29 at the ESRF regularly receive samples in the 50 mm range which are now considered as standard and for which the beamlines were configured. The driving forces to the use of ever smaller samples come from increasing competition between structural biologists, from increasingly challenging projects which may only lead to tiny crystals and from the realization that in some cases microcrystals or micrometre-sized portions of larger crystals provide better ordered crystalline lattices and thus improved diffraction quality.…”

Section: Introductionmentioning

confidence: 99%

“…The complex has been constructed in two phases. The first-phase beamline, ID23-1 (Nurizzo et al, 2006), has been operational since early 2004. The second-phase beamline, ID23-2, with a microfocus beam, has been open to the user community since November 2005.…”

Section: Introductionmentioning

confidence: 99%

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The ID23-2 structural biology microfocus beamline at the ESRF

et al. 2009

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The first phase of the ESRF beamline ID23 to be constructed was ID23-1, a tunable MAD-capable beamline which opened to users in early 2004. The second phase of the beamline to be constructed is ID23-2, a monochromatic microfocus beamline dedicated to macromolecular crystallography experiments. Beamline ID23-2 makes use of well characterized optical elements: a singlebounce silicon (111) monochromator and two mirrors in Kirkpatrick-Baez geometry to focus the X-ray beam. A major design goal of the ID23-2 beamline is to provide a reliable, easy-to-use and routine microfocus beam. ID23-2 started operation in November 2005, as the first beamline dedicated to microfocus macromolecular crystallography. The beamline has taken the standard automated ESRF macromolecular crystallography environment (both hardware and software), allowing users of ID23-2 to be rapidly familiar with the microfocus environment. This paper describes the beamline design, the special considerations taken into account given the microfocus beam, and summarizes the results of the first years of the beamline operation.

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Section: The Id23 X-ray Sourcementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The ID23-2 structural biology microfocus beamline at the ESRF

et al. 2009

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“…The SeMet protein crystallized in space group R32 and contained three molecules in the asymmetric unit. A highly redundant 3.4 Å SeMet anomalous data set was collected at the peak and inflection of the Se-Met signal, as measured by X-ray fluorescence for experimental phasing on ID23-1 (Nurizzo et al 2006) at the European Synchrotron Radiation Facility (ESRF). The native protein crystallized in space group P21, contained four molecules in the asymmetric unit and a data set to 2.4 Å was obtained using the helical data collection procedure on ID29 at the ESRF (de Sanctis et al 2012).…”

Section: Maelstrom Purificationmentioning

confidence: 99%

Metazoan Maelstrom is an RNA-binding protein that has evolved from an ancient nuclease active in protists

Chen

Campbell

Pandey

et al. 2015

RNA

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Piwi-interacting RNAs (piRNAs) guide Piwi argonautes to their transposon targets for silencing. The highly conserved protein Maelstrom is linked to both piRNA biogenesis and effector roles in this pathway. One defining feature of Maelstrom is the predicted MAEL domain of unknown molecular function. Here, we present the first crystal structure of the MAEL domain from Bombyx Maelstrom, which reveals a nuclease fold. The overall architecture resembles that found in Mg 2+ -or Mn 2+ -dependent DEDD nucleases, but a clear distinguishing feature is the presence of a structural Zn 2+ ion coordinated by the conserved ECHC residues. Strikingly, metazoan Maelstrom orthologs across the animal kingdom lack the catalytic DEDD residues, and as we show for Bombyx Maelstrom are inactive as nucleases. However, a MAEL domain-containing protein from amoeba having both sequence motifs (DEDD and ECHC) is robustly active as an exoribonuclease. Finally, we show that the MAEL domain of Bombyx Maelstrom displays a strong affinity for single-stranded RNAs. Our studies suggest that the ancient MAEL nuclease domain evolved to function as an RNA-binding module in metazoan Maelstrom.

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“…The combination of highly intense focused X-ray beams, automatic sample changers, automated beam delivery, online data analysis and fast readout detectors at synchrotron macromolecular crystallography (MX) beamlines now allows for the collection of hundreds of datasets during each assigned experimental session (Arzt et al, 2005;Beteva et al, 2006;Bourenkov & Popov, 2010;Bowler et al, 2010;Cherezov et al, 2009;Cipriani et al, 2006;de Sanctis et al, 2012;Flot et al, 2010;Gabadinho et al, 2010;Incardona et al, 2009;Jacquamet et al, 2009;Leslie et al, 2002;McCarthy et al, 2009;McPhillips et al, 2002;Nurizzo et al, 2006;Soltis et al, 2008). In many cases, complete diffraction datasets can be collected in under one minute (Hü lsen et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Automatic processing of macromolecular crystallography X-ray diffraction data at the ESRF

et al. 2013

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The development of automated high-intensity macromolecular crystallography (MX) beamlines at synchrotron facilities has resulted in a remarkable increase in sample throughput. Developments in X-ray detector technology now mean that complete X-ray diffraction datasets can be collected in less than one minute. Such high-speed collection, and the volumes of data that it produces, often make it difficult for even the most experienced users to cope with the deluge. However, the careful reduction of data during experimental sessions is often necessary for the success of a particular project or as an aid in decision making for subsequent experiments. Automated data reduction pipelines provide a fast and reliable alternative to user-initiated processing at the beamline. In order to provide such a pipeline for the MX user community of the European Synchrotron Radiation Facility (ESRF), a system for the rapid automatic processing of MX diffraction data from single and multiple positions on a single or multiple crystals has been developed. Standard integration and data analysis programs have been incorporated into the ESRF data collection, storage and computing environment, with the final results stored and displayed in an intuitive manner in the ISPyB (information system for protein crystallography beamlines) database, from which they are also available for download. In some cases, experimental phase information can be automatically determined from the processed data. Here, the system is described in detail.

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The ID23-1 structural biology beamline at the ESRF

Cited by 157 publications

References 21 publications

The ID23-2 structural biology microfocus beamline at the ESRF

The ID23-2 structural biology microfocus beamline at the ESRF

Metazoan Maelstrom is an RNA-binding protein that has evolved from an ancient nuclease active in protists

Automatic processing of macromolecular crystallography X-ray diffraction data at the ESRF

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