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18 citations found for Ryan, T.
Search for Ryan, T. in the World Directory of Crystallographers
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BIOLOGY | MEDICINE
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Small-angle X-ray scattering and tryptophan fluorescence studies of phosphoethanolamine transferase (EptA) suggest conformational flexibility linked to enzyme activity.
PHYSICS | FELs
The theory of preferred orientation in fluctuation scattering is developed and demonstrated in experimental studies of self-assembled lipid materials.
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The factors influencing the homogeneity of the incident X-ray beam when a graphite monochromator is applied are discussed, in particular the influence of the size and shape of the focal spot of the X-ray tube and the diffraction angle of the monochromator. Beam profiles have been measured for several commonly used X-ray tubes - with a fine or normal focus - and compared. It is shown that in certain cases the normal-focus X-ray tubes give a much broader high- intensity region of the incident beam than the fine- focus X-ray tubes.
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Coflow is a new method for delivering radiation-sensitive biological and other solution-based samples to high-brightness X-ray beamlines that exploits laminar flow to ameliorate radiation-damage limitations and provides a host of practical improvements associated with these types of experiments.
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Size exclusion chromatography (SEC) small-angle X-ray scattering (SAXS) is a powerful structural biology tool where the best outcomes are obtained through an optimized experimental approach. Optimization of SEC and integration of a sheath flow sample environment into the Australian Synchrotron's SAXS/WAXS beamline has greatly improved data quality and the ability to deal with difficult protein samples.
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Small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) measurements of five standard proteins in solution using 12 SAXS and four SANS instruments demonstrate reproducibility and yield consensus scattering profiles that provide a foundation benchmarking set to evaluate approaches to scattering-profile prediction from atomic coordinates.
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Updated guidelines are presented for publishing biomolecular small-angle scattering (SAS) experiments so that readers can independently assess the quality of the data and models presented. The focus is on solution scattering experiments with either X-rays (SAXS) or neutrons (SANS), where the primary goal is the generation and testing of three-dimensional models, particularly in the context of integrative/hybrid structural modelling.
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