Pilatus3 s 6m

Manufactured by Dectris

The Pilatus3 S 6M is a high-performance X-ray detector designed for a wide range of scientific applications. It features a large active area of 83.8 x 70.0 mm² and a pixel size of 172 x 172 μm². The detector offers a high frame rate of up to 300 Hz and a high dynamic range, making it suitable for a variety of X-ray imaging and diffraction experiments.

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Lab products found in correlation

Intelli plate, by Hampton Research (1 mentions) Jcsg core suite, by Qiagen (1 mentions) Cryschem plate, by Hampton Research (1 mentions) Nucleix, by Qiagen (1 mentions)

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Pilatus3 6M (7 citations) Pilatus3 S 6M detector (2 citations)

2 protocols using pilatus3 s 6m

Structural Determination of LbaCas13a-crRNA Complex

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Initial screening was carried out with JCSG Core Suites (Qiagen) in
96-well sitting drop vapor diffusion format (Intelli-plate, Hampton Research) at
293 ± 1 K. Diffraction-quality crystals of the LbaCas13a:crRNA complex
(20-nt and 24-nt containing spacer) (A₂₈₀=4.0) and
LbaCas13a:pre-crRNA complex (24-nt containing spacer)
(A₂₈₀=5.7) grew in 0.2 M ammonium iodide and 20%
(w/v) PEG 3,350. Crystals were cryoprotected in 10–15% (v/v)
glycerol, and high-resolution diffraction data were collected at the Advanced
Light Source (ALS) beam line 8.3.1 on a Pilatus3 S 6M (Dectris) detector under
cryogenic conditions. To produce isomorphous crystals for phasing by native
single-anomalous dispersion (SAD), sitting drop vapor diffusion experiments
containing 2 μL purified LbaCas13a:crRNA complex (24-nt containing
spacer) complex (A₂₈₀=4.0) and 2 μL reservoir
solution (0.2 M ammonium iodide, 20–25% (w/v) PEG 3,350) were
prepared in 24-well Cryschem plates (Hampton Research). A total of 52 datasets
were collected from 26 crystals (cryoprotected in 10% (v/v) glycerol)
under cryogenic conditions at 6.0 keV (ALS beam line 8.3.1, Pilatus3 S 6M). Each
dataset covered 360° of crystal rotation divided into 0.2°
images collected in 45° inverse-beam wedges at 5 Hz. To minimize pixel
readout error, the detector was moved by 10 mm before collecting a second
360°-pass from the same position of each crystal.

Knott G.J., East-Seletsky A., Cofsky J.C., Holton J.M., Charles E., O’Connell M.R, & Doudna J.A. (2017). Guide-bound structures of an RNA-targeting A-cleaving CRISPR-Cas13a enzyme. Nature structural & molecular biology, 24(10), 825-833.

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Protein Crystal Structure Determination

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Initial screens were performed using Nucleix and Protein Complex suites (Qiagen) in a sitting-drop setup, with 200 nL of sample added to 200 nL of reservoir solution by a Mosquito instrument (SPT Labtech) and incubated at either 4°C or 20°C. Several conditions yielded crystals within one day, and initial hits were further optimized at a larger scale. The crystal used for the final dataset was produced as follows: 0.5 μL of sample was combined with 0.5 μL reservoir solution (0.05 M sodium succinate (pH 5.3), 0.5 mM spermine, 20 mM magnesium chloride, 2.6 M ammonium sulfate) in a hanging-drop setup over 500 μL reservoir solution, and the tray was stored at 20°C. Crystals formed within one day and remained stable for the 2.5 weeks between tray setting and crystal freezing. A crystal was looped, submerged in cryoprotection solution (0.05 M sodium succinate (pH 5.3), 0.5 mM spermine, 20 mM magnesium chloride, 3 M ammonium sulfate) for a few seconds, and frozen in liquid nitrogen. Diffraction data were collected under cryogenic conditions at the Advanced Light Source beamline 8.3.1 on a Pilatus3 S 6M (Dectris) detector.

Cofsky J.C., Knott G.J., Gee C.L, & Doudna J.A. (2022). Crystal structure of an RNA/DNA strand exchange junction. PLoS ONE, 17(4), e0263547.

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