X 16m detector

Manufactured by Dectris

The X 16M detector is a high-performance, large-area detector designed for advanced scientific applications. It features a 16-megapixel sensor with a large active area, delivering high-resolution imaging capabilities. The detector is engineered to provide reliable and accurate data acquisition, catering to the needs of researchers and scientific institutions.

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Lab products found in correlation

Pymol v2, by Schrödinger (2 mentions) X 9 m detector, by Dectris (1 mentions)

3 protocols using x 16m detector

Structural Determination of crPTEN Variants

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n-crPTEN-13_sp-T1, 4p-crPTEN-13_sp-T2 and 4p-crPTEN-20_sp-T3 data were collected at National Synchrotron Light Source-II at beamlines 17-ID-1(AMX) on a DECTRIS Eiger X 9M detector and 17-ID-2 (FMX) on a DECTRIS Eiger X 16M detector. n-crPTEN-13_sp-T1, 4p-crPTEN-13_sp-T2 were collected using a vector over the length of the crystal. 4p-crPTEN-20_sp-T3 data were collected using crystals ranging in sizes from 10-13 μm using multiple crystals mounted in a single loop⁵⁵. Three data sets were scaled using XSCALE with a resolution cut-off criterion was 〈I/σ(I)〉 of 2.9 Å. Datasets were indexed, integrated and scaled using fastdp^{56 (link)}, XDS^{57 (link)}, and aimless⁵⁸ (Table S1). The structure for the n-crPTEN-13_sp-T1, 4p-crPTEN-13_sp-T2 and 4p-crPTEN-20_sp-T3 were determined by direct refinement using PDB ID 1D5R ⁵⁹ as the starting model. The data were refined using iterative rounds of refinement with REFMAC5^{60 ,61 (link)} and manual rebuilding in Coot^{62 (link)}. Structures were validated using Coot^{62 (link)} and PDB Deposition tools with more than 95 % of residues in preferred and allowed regions according to Ramachandran statistics (Table S1). Figures were rendered in PyMOL (v2.2.3, Schrödinger, LLC, New York, NY). Buried areas were calculated with PDBePISA^{63 (link)}.

Dempsey D.R., Viennet T., Park E., Henriquez S., Chen Z., Jeliazkov J.R., Phan K.L., Coote P., Gray J.J., Eck M.J., Gabelli S.B., Arthanari H, & Cole P.A. (2021). The Structural Basis of PTEN Regulation by Multi-Site Phosphorylation. Nature structural & molecular biology, 28(10), 858-868.

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Helium Path for EIGER X 16M Detector

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The FMX beamline is equipped with a DECTRIS EIGER X 16M detector, which has a detector shield to prevent accidental damage. To fit the detector size and to reduce air scattering and absorption for our experiments at 5 keV, we developed a pyramidal plastic helium path as shown in Fig. 1 ▸(a). The helium path is mounted on a frame surrounding the detector housing. It features an inlet on top and an outlet at the bottom of the chamber for helium flow, an oxygen sensor to verify fill levels, and one thin X-ray transparent Kapton window (7.62 µm thickness) on the upstream sample end. The distance between sample and detector is fixed at 137 mm, corresponding to a diffraction limit (d_min) of 2.9 Å at the detector edge, and 2.5 Å in the detector corner for the 5 keV experiments. The beamline tungsten beamstop is 5 mm thick and is placed at a distance of 5 mm after the sample and 2 mm before the Kapton window (45 × 45 mm). So, the distance from the sample to the window is 12 mm in the beam direction.

Karasawa A., Andi B., Fuchs M.R., Shi W., McSweeney S., Hendrickson W.A, & Liu Q. (2022). Multi-crystal native-SAD phasing at 5 keV with a helium environment. IUCrJ, 9(Pt 6), 768-777.

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Structural Characterization of p53R175H-HLA-A*02:01 Complex

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Crystals of the ternary complex H2-Fab–p53^R175H/HLA-A*02:01 were grown by vapor diffusion in hanging drops set up with a TTP mosquito robot with a reservoir solution of 0.2 M ammonium chloride and 20% (w/v) PEG 3350 MME. Crystals were flash-cooled in mother liquor. Data were collected at National Synchrotron Light Source-II at beamlines 17-ID-1(AMX) on a Dectris EIGER X 16M detector. The dataset was indexed, integrated, and scaled using fastdp (67 (link)), XDS (68 (link)), and aimless (69 (link)). Monoclinic crystals of H2-Fab–p53^R175H/HLA-A*02:01 diffracted to 3.5 Å. The structure for the H2-Fab-p53^R175H/HLA-A*02:01 complex was determined by molecular replacement with PHASER (70 (link)) using PDB ID 6O4Y (71 (link)) and 6UJ9 as the search models. The data were refined to a final resolution of 3.5 Å using iterative rounds of refinement with REFMAC5 (72 (link), 73 (link)) and manual rebuilding in Coot (74 (link)). Structures were validated using Coot and PDB Deposition tools. The model has 95.2% of the residues in preferred and 3.8% in allowed regions according to Ramachandran statistics (table S4). Figures were rendered in PyMOL (v2.2.3, Schrödinger, LLC). Buried areas were calculated with PDBePISA (37 (link)). The docking angle that determines the relative orientation between the pHLA and the Fab/TCR was calculated by the web server TCR3d (75 (link), 76 (link)).

Hsiue E.H., Wright K.M., Douglass J., Hwang M.S., Mog B.J., Pearlman A.H., Paul S., DiNapoli S.R., Konig M.F., Wang Q., Schaefer A., Miller M.S., Skora A.D., Azurmendi P.A., Murphy M.B., Liu Q., Watson E., Li Y., Pardoll D.M., Bettegowda C., Papadopoulos N., Kinzler K.W., Vogelstein B., Gabelli S.B, & Zhou S. (2021). Targeting a neoantigen derived from a common TP53 mutation. Science (New York, N.Y.), 371(6533), eabc8697.

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