A crystal structure refinement from Laue photographs taken with synchrotron radiation

Wood, I. G.; Thompson, Paul; Matthewman, J. C.

doi:10.1107/s0108768183002931

Cited by 42 publications

(11 citation statements)

References 3 publications

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“…We were not the only ones encountering this problem. Laue diffraction patterns from single crystals of an aluminium phosphate had also been obtained with short exposures at the new Synchrotron Radiation Source at Daresbury Laboratory by Wood et al [13], and its structure successfully refined. Also at Daresbury, the protein crystallographer John Helliwell and his colleagues were commissioning beamline SRS9.6 for protein crystallography, similar to our beamlines at CHESS.…”

Section: Synchrotrons the Redevelopment Of Laue Diffraction And Time-resolved Crystallographymentioning

confidence: 99%

Laue diffraction and time-resolved crystallography: a personal history

Moffat

2019

Phil. Trans. R. Soc. A.

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A personal, historical view is presented of Laue X-ray diffraction and its application to time-resolved studies of dynamic processes, largely in light-sensitive biological systems. In Laue diffraction, a stationary crystal is illuminated by a polychromatic X-ray source. Laue diffraction has inherent complications largely absent in monochromatic diffraction, and consequently fell into disuse for quantitative structure determination. However, the advent of naturally polychromatic, intense, pulsed storage ring X-ray sources in the 1970s led to re-examination at Daresbury and elsewhere of its underlying principles. Laue diffraction has been successfully applied at storage ring sources to time-resolved, pump–probe crystallographic studies, whose exposure time and time resolution were progressively reduced from minutes to seconds, milliseconds, nanoseconds and 100 ps. Most recently, hard X-ray free electron laser sources have been used to generate narrow bandpass Laue diffraction patterns. The femtosecond X-ray pulses from such sources are completely destructive, generate only one diffraction pattern per tiny crystal and have unusual properties. However, they too are being applied to time-resolved crystallography to explore, for example, isomerization and rapid tertiary structural changes on the chemical, femtosecond timescale. This article is part of the theme issue ‘Fifty years of synchrotron science: achievements and opportunities’.

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Section: Synchrotrons the Redevelopment Of Laue Diffraction And Time-resolved Crystallographymentioning

confidence: 99%

Laue diffraction and time-resolved crystallography: a personal history

Moffat

2019

Phil. Trans. R. Soc. A.

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“…All synchrotron sources are n atu rally polychrom atic and therefore ap p ro p riate to the Laue technique (Amoros et a l . 1975;Wood et al 1983;Moffat et al 1 1985;H ajdu et al 1987). The exposure tim e in a Laue experim ent is inversely proportional to the spectral intensity falling on the crystal, in units such as photons (s m m 2 0.1 % bandpass)"1.…”

Section: The Time-resolved Experiments (A) X -Ray Source and Opticsmentioning

confidence: 99%

Time-resolved crystallography: principles, problems and practice

Moffatt

Chen

et al. 1992

Phil. Trans. R. Soc. Lond. A

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Time-resolved crystallography is founded on the belief that a complete understanding of mechanism at the molecular level demands knowledge, not just of long-lived, readily observable structures, but also of short-lived intermediates in processes such as catalysis, ligand binding and release, and protein unfolding. Synchrotron X-ray sources enable X -ray diffraction patterns of high quality to be obtained from single crystals with exposure times that are often commensurate with the lifetime of the desired intermediates. The basic tools are therefore in place. How shall they be applied effectively? Can crystallography, long regarded as a static technique, in fact encompass dynamic processes? What pitfalls remain to be overcome? A time-resolved crystallographic experiment has five main components: the X -ray source; reaction initiation; reaction monitoring by optical or other techniques; X-ray data acquisition in real time; and data reduction and analysis. These are illustrated by our recent work on photoactive yellow protein, and on the acquisition and analysis of crystallographic data using 120 ps exposures.

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“…(i) The use of a silicon standard crystal and a film in a pilot study on aluminium phosphate (Wood et al 1983).…”

Section: L(h)= K G (Adx)\f (H)\\ (6)mentioning

confidence: 99%

The emergence of the synchrotron Laue method for rapid data collection from protein crystals

Cassetta

Deacon

Emmerich

et al. 1993

Proc. R. Soc. Lond. A

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Synchrotron X-radiation (SR) is intense, polychromatic and collimated. It is widely exploited, in macromolecular crystallography, particularly using a monochromatized short wavelength beam. The spectral curve of SR, however, ideally lends itself to use of Laue geometry, i. e. the original diffraction experimental arrangement based on a stationary crystal and a polychromatic X-ray beam. Rapid exposure times and time-resolved crystallography studies, e. g. of enzymes, are now possible. Historical objections to the use of Laue diffraction data, particularly the multiplicity distribution, have been found not to be as limiting as once thought. The credentials of the Laue method have been established through a variety of Laue crystal structure analyses, involving photographic film as detector. Recently a three-dimensional arrangement of films, known as a toast-rack, has been used to alleviate problems with spatially overlapping spots. This paper provides a review of these results and then reports several developments. In particular, one of the first Laue analyses using an image plate as detector, namely of a cobalt substituted concanavalin A crystal, is discussed. Recent experimental developments, also at the Daresbury synchrotron, are then described. First, a large toast-rack has been used to record Laue data from a protein crystal. Secondly, a transmission X-ray mirror has been constructed from thin mylar (1.5 μm) and used to provide a λ max filter instead of using aluminium foils. Thirdly, since the Laue method suffers from poor sampling of the low resolution data, a new method (known as LOT) has been introduced.

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A crystal structure refinement from Laue photographs taken with synchrotron radiation

Cited by 42 publications

References 3 publications

Laue diffraction and time-resolved crystallography: a personal history

Laue diffraction and time-resolved crystallography: a personal history

Time-resolved crystallography: principles, problems and practice

The emergence of the synchrotron Laue method for rapid data collection from protein crystals

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