The ID23-2 structural biology microfocus beamline at the ESRF

Flot, David; Mairs, Trevor; Giraud, Thierry; Guijarro, Matias; Lesourd, M.; Rey, Vicente; Brussel, Denis van; Morawe, Christian; Borel, Christine; Hignette, O.; Chavanne, J.; Nurizzo, Didier; McSweeney, Seán; Mitchell, Edward P.

doi:10.1107/s0909049509041168

Cited by 200 publications

(153 citation statements)

References 38 publications

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“…Moreover a helical data collection mode was selected to minimize exposure to X-rays and thus radiation damage (Flot et al, 2010). Appropriate data collection segments were determined using STRATEGY routine of MOSFLM (Leslie, 1992) and collected using 2.3°oscillation for a complete range of 180°.…”

Section: Data Collection and Treatmentmentioning

confidence: 99%

Rotor architecture in the yeast and bovine F1-c-ring complexes of F-ATP synthase

Giraud

Paumard

Sanchez

et al. 2012

Journal of Structural Biology

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Section: Data Collection and Treatmentmentioning

confidence: 99%

Rotor architecture in the yeast and bovine F1-c-ring complexes of F-ATP synthase

Giraud

Paumard

Sanchez

et al. 2012

Journal of Structural Biology

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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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“…Monte Carlo simulations of photoelectron trajectories predicted that the greatest energy deposition in the photoelectron flight path was a few microns from the photoelectron origin, and that the photoelectrons would escape the illuminated crystal volume if the crystal (18) or the beam (19) were small relative to the photoelectron path length. Thus, there is a potential for reducing radiation damage if the incident X-ray beam size is decreased beyond the microbeams now in use, which are as small as 5-10 μm (20)(21)(22). Photoelectron transfer of energy out of the beam footprint causing "penumbral damage" is well known in radiology and has been observed in studies with high-energy (MeV) X-rays (23).…”

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confidence: 99%

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam

Sanishvili

Yoder

Pothineni

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

123

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Radiation damage is a major limitation in crystallography of biological macromolecules, even for cryocooled samples, and is particularly acute in microdiffraction. For the X-ray energies most commonly used for protein crystallography at synchrotron sources, photoelectrons are the predominant source of radiation damage. If the beam size is small relative to the photoelectron path length, then the photoelectron may escape the beam footprint, resulting in less damage in the illuminated volume. Thus, it may be possible to exploit this phenomenon to reduce radiation-induced damage during data measurement for techniques such as diffraction, spectroscopy, and imaging that use X-rays to probe both crystalline and noncrystalline biological samples. In a systematic and direct experimental demonstration of reduced radiation damage in protein crystals with small beams, damage was measured as a function of micron-sized X-ray beams of decreasing dimensions. The damage rate normalized for dose was reduced by a factor of three from the largest (15.6 μm) to the smallest (0.84 μm) X-ray beam used. Radiation-induced damage to protein crystals was also mapped parallel and perpendicular to the polarization direction of an incident 1-μm X-ray beam. Damage was greatest at the beam center and decreased monotonically to zero at a distance of about 4 μm, establishing the range of photoelectrons. The observed damage is less anisotropic than photoelectron emission probability, consistent with photoelectron trajectory simulations. These experimental results provide the basis for data collection protocols to mitigate with micron-sized X-ray beams the effects of radiation damage.microcrystallography | synchrotron radiation T he brilliance of synchrotron radiation from undulator devices on third-generation sources has been an enormous boon to crystallography of biological macromolecules. The high flux density and low divergence of undulator beams led to a rapid decrease in the minimum crystal size and minimum beam size that can yield usable diffraction data (1-4). However, the resulting decrease in diffracting volume necessitates an increase in X-ray exposure per unit sample volume, increasing radiation damage and severely compromising the substantial benefits of brilliant undulator sources. Thus, there is considerable interest in understanding the mechanism and spatial extent of X-rayinduced damage to crystals of biological macromolecules.Diffraction experiments are typically performed at cryotemperatures (approximately 100 K) to prevent the diffusion of free radicals, which are a major source of damage in crystals exposed to X-rays at higher temperatures (5), but cryocooling does not eliminate X-ray damage. Many experimental approaches to circumventing the effects of radiation damage have been investigated (6-10) but have not yet yielded a breakthrough result. Zero-dose diffraction intensities have been extrapolated from measured values by mathematical modeling (7-9). The effects of radiation damage have also been exploited for crystallograp...

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The ID23-2 structural biology microfocus beamline at the ESRF

Cited by 200 publications

References 38 publications

Rotor architecture in the yeast and bovine F1-c-ring complexes of F-ATP synthase

Rotor architecture in the yeast and bovine F1-c-ring complexes of F-ATP synthase

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

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam

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