PILATUS: A single photon counting pixel detector for X-ray applications

Henrich, B.; Bergamaschi, A.; Broennimann, Ch.; Dinapoli, R.; Eikenberry, Eric F.; Johnson, I.; Kobas, M.; Kraft, Philipp; Mozzanica, A.; Schmitt, B.

doi:10.1016/j.nima.2009.03.200

Cited by 280 publications

(204 citation statements)

References 6 publications

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“…Correction for detector-sensitivity variation is an instrument-specific procedure, the details of which vary for different detector types. For pixel-array detectors (Henrich et al, 2009), one relevant factor is the probability of recording an individual scattered photon. In particular, the sensor has a fixed thickness of, for example, crystalline silicon (typically between 320 mm and 1 mm), giving rise to a specific probability of a photon being absorbed by the sensor, dependent on the wavelength of the photon and the incident angle,…”

Section: Research Papersmentioning

confidence: 99%

“…In more recent years there has been a step change in MX throughput, driven principally by the availability of new X-ray sources and data-collection methodologies (Emma et al, 2010;Ishikawa et al, 2012;White et al, 2012;Gati et al, 2014;Stellato et al, 2014;Sierra et al, 2016;Fuller et al, 2017), highframe-rate pixel-array detectors (Henrich et al, 2009), fast sample exchange (Russi et al, 2016) and automated data analysis (Winter, 2010;Winter & McAuley, 2011;Vonrhein et al, 2011). This allows larger numbers of smaller samples to be used, with correspondingly more challenging data.…”

Section: Introductionmentioning

confidence: 99%

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DIALS: implementation and evaluation of a new integration package

Winter

Waterman

Parkhurst

et al. 2018

Acta Cryst Sect D Struct Biol

890

797

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The DIALS project is a collaboration between Diamond Light Source, Lawrence Berkeley National Laboratory and CCP4 to develop a new software suite for the analysis of crystallographic X-ray diffraction data, initially encompassing spot finding, indexing, refinement and integration. The design, core algorithms and structure of the software are introduced, alongside results from the analysis of data from biological and chemical crystallography experiments.

show abstract

Section: Research Papersmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

DIALS: implementation and evaluation of a new integration package

Winter

Waterman

Parkhurst

et al. 2018

Acta Cryst Sect D Struct Biol

890

797

View full text Add to dashboard Cite

show abstract

“…SAXS patterns were recorded with a Pilatus 300k positionsensitive detector (Dectris Ltd, Switzerland) [44]. Later, SAXS was re-measured with a Pilatus 1M detector [45][46]. The beam used was point-collimated (1×0.7 mm) and monochromatized to 9.6 keV or 12 keV (repeated SAXS measurement) with a Si (311) double crystal monochromator.…”

Section: Small-and Wide-angle X-ray Scatteringmentioning

confidence: 99%

A mechanistic view of lipid membrane disrupting effect of PAMAM dendrimers

Berényi

Mihály

Wacha

et al. 2014

Colloids and Surfaces B: Biointerfaces

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The effect of 5 th generation polyamidoamine (PAMAM G5) dendrimers on multilamellar dipalmitoylphosphocholine (DPPC) vesicles was investigated. PAMAM was added in two different concentration to the lipids (10 -3 and 10 -2 dendrimer/lipid molar ratios). The thermal behavior of the evolved systems was characterized by DSC; while the structure and the morphology were investigated with small-and wide-angel X-ray scattering (SWAXS), freeze-fracture electron microscopy (FFTEM) and phosphorus-31 nuclear magnetic resonance ( 31 P-NMR) spectroscopy, respectively. IR spectroscopy was used to study the molecular interactions between PAMAM and DPPC. The obtained results show that the dendrimers added in 10 -3 molar ratio to the lipids generate minor perturbations in the multilamellar structure and thermal character of liposomes, while added in 10 -2 molar ratio dendrimers cause major disturbance in the vesicular system. The terminal amino groups of the dendrimers are in strong interaction with the phosphate headgroups and through this binding dendrimers disrupt the regular multilamellar structure of DPPC. Besides highly swollen, fragmented bilayers, small vesicles are formed.

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“…The scattered X-rays were transported through an evacuated flight tube to the detector, which was placed 7.2 m behind the sample. The detector 23 was a Pilatus 2M, with 1675 Â 1475 square pixels of 172 mm size, and was protected from the direct beam by a central beamstop. The X-ray beam diameter at the detector position, measured with an attenuated beam and without inserted sample, corresponded to 3-4 detector pixels.…”

Section: Methodsmentioning

confidence: 99%

Two-dimensional structure from random multiparticle X-ray scattering images using cross-correlations

et al. 2013

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Knowledge of the structure of biological macromolecules, especially in their native environment, is crucial because of the close structure-function relationship. X-ray small-angle scattering is used to determine the shape of particles in solution, but the achievable resolution is limited owing to averaging over particle orientations. In 1977, Kam proposed to obtain additional structural information from the cross-correlation of the scattering intensities. Here we develop the method in two dimensions, and give a procedure by which the single-particle diffraction pattern is extracted in a model-independent way from the correlations. We demonstrate its application to a large set of synchrotron X-ray scattering images on ensembles of identical, randomly oriented particles of 350 or 200 nm in size. The obtained 15 nm resolution in the reconstructed shape is independent of the number of scatterers. The results are discussed in view of proposed 'snapshot' scattering by molecules in the liquid phase at X-ray free-electron lasers.

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PILATUS: A single photon counting pixel detector for X-ray applications

Cited by 280 publications

References 6 publications

DIALS: implementation and evaluation of a new integration package

DIALS: implementation and evaluation of a new integration package

A mechanistic view of lipid membrane disrupting effect of PAMAM dendrimers

Two-dimensional structure from random multiparticle X-ray scattering images using cross-correlations

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