Eiger detector

Manufactured by Dectris

Sourced in France, Switzerland

The Eiger detector is a high-performance X-ray detector developed by Dectris. It is designed to capture and analyze X-ray data for scientific and industrial applications. The Eiger detector offers fast readout, high resolution, and advanced features to facilitate precise X-ray measurements and analysis.

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Lab products found in correlation

D8 advance diffractometer, by Bruker (1 mentions) Pymol molecular graphic system, by Schrödinger (1 mentions)

Spelling variants of this product

Eiger 16M detector (22 citations) EIGER X 16 M detector (16 citations) Eiger 4M detector (11 citations) Eiger 9M detector (7 citations) Eiger 1 M detector (7 citations) Eiger 16M PIXEL detector (4 citations) Eiger R 1 M detector system (3 citations) EIGER X 1M detector (3 citations) EIGER hybrid photon-counting (HPC) pixel-array detector (2 citations) EIGER 2 × 4 M detector (2 citations)

8 protocols using eiger detector

Small-Angle X-Ray Scattering Analysis

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Small-angle X-ray scattering data
were collected with a sample–detector distance of 562 mm from
an Anton Paar SAXSpoint 2.0 instrument using a Cu Kα radiation
source (λ = 1.54 Å). Two-dimensional (2D) scattering patterns
were acquired on a Dectris Eiger detector and reduced by azimuthal
integration into one-dimensional (1D) radial profiles of intensity
against the scattering vector using Anton Paar SAXSAnalysis software.

Bowley E., Liu W., Adams D.J, & Squires A.M. (2024). Soft Materials with Time-Programmed Changes in Physical Properties through Lyotropic Phase Transitions Induced by pH-Changing Reactions. ACS Applied Materials & Interfaces, 16(15), 19585-19593.

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Quantitative Phase Analysis of Cement Paste

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The same paste prepared for the calorimetry measurement (PC-52.5-w/c = 0.40) was used to fill the capillaries of ~1 mm in diameter. LXRPD measurements were collected on a D8 ADVANCE diffractometer (Bruker AXS) using strictly monochromatic Mo-Kα₁ radiation (λ = 0.7093 Å). This diffractometer is located at SCAI, University of Malaga. The incident beam was formed by a primary monochromator with a focusing mirror and a 2 mm anti-scatter slit. Moreover, 2.5° Soller slits were used for the incident and transmitted beams. An EIGER detector (from DECTRIS, Baden, Switzerland) was used which is optimised for Mo anodes. This was used with an aperture of 4 × 21 degrees, working in VDO mode. Data collection was performed from 3 to 35° (2θ) for 2 h and 10 min. Rietveld quantitative phase analysis was performed with GSAS software.

Shirani S., Cuesta A., Morales-Cantero A., Santacruz I., Diaz A., Trtik P., Holler M., Rack A., Lukic B., Brun E., Salcedo I.R, & Aranda M.A. (2023). 4D nanoimaging of early age cement hydration. Nature Communications, 14, 2652.

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Structural Characterization of Scribble/PDZ1:TMIGD1 Complex

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All diffraction data were collected on the MX2 beamline at the Australian Synchrotron using an Eiger detector (Dectris, Baden-Dättwil, Switzerland) with an oscillation range of 0.1° per frame using a wavelength of 0.9537 Å. Diffraction data was integrated using DIALS and scaled with AIMLESS^{89 (link)–91 (link)}. The structure of Scribble/PDZ1:TMIGD1 peptide complex was solved by molecular replacement with Phaser using human Scribble PDZ1:human APC (PDB ID: 6XA8)^{40 (link)} as the search model^{92 (link)}. The molecular replacement solution was manually rebuilt using Coot and refined with PHENIX^{93 (link),94 (link)}. Data collection and refinement statistics are summarised in Supplementary Table 1. Final images of Scrib/PDZ1:TMIGD1 peptide complex were generated using the PyMOL molecular graphic system, version 1.8.6 (Schrödinger, LLC, New York, USA) and all software was accessed through SBGrid suite^{95 (link)}. All raw diffraction images were deposited on the SBGrid Data Bank^{96 (link)} using the PDB accession code 8CD3.

Thüring E.M., Hartmann C., Maddumage J.C., Javorsky A., Michels B.E., Gerke V., Banks L., Humbert P.O., Kvansakul M, & Ebnet K. (2023). Membrane recruitment of the polarity protein Scribble by the cell adhesion receptor TMIGD1. Communications Biology, 6, 702.

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Structural Determination of Protein Complex

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Data were collected on beamline PROXIMA 2 A (Soleil Synchrotron, Saint Aubin, France) using an Eiger detector (Dectris), respectively, indexed and integrated with XDS^{52 (link)}. All the structural models were iteratively built-in COOT^{53 (link)} with a structural model (PDB ID: 5JMN)^{54 (link)} and refined with REFMAC5 in CCP4i v7^{55 (link)}. The structure was validated with MolProbity v4.5^{56 (link)}. Polder electron density maps were calculated by phenix.polder^{57 (link)}. All figures were generated by Pymol (Schrödinger LLC).

Plé C., Tam H.K., Vieira Da Cruz A., Compagne N., Jiménez-Castellanos J.C., Müller R.T., Pradel E., Foong W.E., Malloci G., Ballée A., Kirchner M.A., Moshfegh P., Herledan A., Herrmann A., Deprez B., Willand N., Vargiu A.V., Pos K.M., Flipo M, & Hartkoorn R.C. (2022). Pyridylpiperazine-based allosteric inhibitors of RND-type multidrug efflux pumps. Nature Communications, 13, 115.

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Structure Determination of AbTetR

Cited 1 time

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Datasets were collected on beam line Proxima 2A at the Soleil Synchrotron, Saint-Aubin, France using a Eiger detector (Dectris), and subsequently indexed and integrated with XDS (Kabsch, 2010 (link)). A molecular replacement solution for wildtype AbTetR was obtained using MrBUMP (Keegan and Winn, 2008 (link)) using a modified structure by Sculptor (Bunkóczi and Read, 2011 (link)) of TetR(D) variant (1A6I) (Orth et al., 1998 (link)) as a search model. Structural models were built in COOT (Emsley et al., 2010 (link)), refined with REFMAC5 (Murshudov et al., 2011 (link)) and validated with MolProbity (Chen et al., 2010 (link)). 100% of the residues are in favored regions of the Ramachandran plot for both structures reported in this manuscript. Polder electron density maps were calculated using phenix.polder (Liebschner et al., 2017 (link)).

Sumyk M., Himpich S., Foong W.E., Herrmann A., Pos K.M, & Tam H.K. (2021). Binding of Tetracyclines to Acinetobacter baumannii TetR Involves Two Arginines as Specificity Determinants. Frontiers in Microbiology, 12, 711158.

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Structural Determination of Bracelet Cyclotides

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X-ray diffraction data were collected on the MX1 and MX2 microfocus beamlines at the Australian Synchrotron and recorded with a Dectris EIGER detector. All the data collected were indexed and integrated by AutoXDS and scaled using Aimless. Crystal structures of the bracelet cyclotides and their variants were solved by molecular replacement using Phaser with the NMR solution structure of cyO2 (PDB ID: 2KNM) as the initial model. Crystallographic structure refinements were performed using PHENIX suite. The refined models were manually rebuilt using Coot guided by Fo-Fc difference maps. Data collection and refinement statistics are summarized in Table S1. All structure images were generated using PyMOL. The final refined structures of cyO2 quasi-racemate, [I11L]cyO2 racemate, [I11G]cyO2 quasi-racemate, hyen D quasi-racemate, [I11L]hD racemate, and [I11G]hD quasi-racemate have been deposited in the Protein Data Bank with the following codes 7RMQ, 7RMR, 7RMS, 7RIH, 7RII, and 7RIJ, respectively.

Huang Y.H., Du Q., Jiang Z., King G.J., Collins B.M., Wang C.K, & Craik D.J. (2021). Enabling Efficient Folding and High-Resolution Crystallographic Analysis of Bracelet Cyclotides. Molecules, 26(18), 5554.

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Structural Characterization of CtRoco Proteins

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The protocols used for the production of the Roco protein from Chlorobium tepidum (CtRoco), the CtRoc-COR and the CtLRR-Roc-COR proteins, and the crystallization and the data collection of the CtLRR-Roc-COR protein have been described previously [5, 25, (link)26] (link). In brief, recombinant protein expression was performed starting from the open reading frames cloned in pProEX plasmids and transformed in Escherichia coli BL21 (DE3) cells. All proteins were purified using a three-step protocol consisting of metal chelate affinity chromatography on Ni-NTA, anion exchange chromatography on a source Q30 column and size-exclusion chromatography on a Superdex 200 column. Before setting up the crystals, the protein was made nucleotide-free by adding an excess of EDTA and loading it on a S200 26/60 gel filtration column equilibrated with 20 mM Hepes ( pH 7.5), 150 mM NaCl, 1 mM DTT and 5% glycerol. Afterwards, 5 mM MgCl 2 was added to the protein and the nucleotide-load was determined using reversed-phase chromatography coupled to HPLC. Crystals were obtained in 0.8 M sodium formate, 0.1 M sodium acetate ( pH 5.5), 10% PEG8000 and 10% PEG1000, and data collection was performed at the PROXIMA2 beamline of the SOLEIL synchrotron (Paris, France) using an EIGER detector (Dectris) [26] (link).

Deyaert E., Leemans M., Singh R.K., Gallardo R., Steyaert J., Kortholt A., Lauer J, & Versées W. (2019). Structure and nucleotide-induced conformational dynamics of the Chlorobium tepidum Roco protein. The Biochemical journal, 476(1).

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Crystallization and X-ray Diffraction of N-Wag31

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Crystals of N-Wag31 were grown by both hanging- and sitting-drop vapour-diffusion methods at 19°C in 0.2 M magnesium chloride, 0.1 M sodium cacodylate at pH 6.5 and 50%(v/v) polyethylene glycol 200. These crystals were very small and recalcitrant to growth. Crystals were flash frozen in liquid nitrogen without any additional cryo-protectant and transported to the European Synchrotron Radiation Facility (ESRF) in France. X-ray diffraction data from an N-Wag31 crystal were collected at the microfocus beamline ID30A-3 (MASSIF-3) at ESRF, which is suitable for such small crystals. Only one useful dataset was obtained after testing 37 crystals. Data collection was carried out at 100 K, using an EIGER detector (DECTRIS Ltd). Data indexing, processing, merging and scaling were performed using XDS (Kabsch, 2010 ▸ ) and the CCP4 suite of software (Winn et al., 2011 ▸ ).

Choukate K, & Chaudhuri B. (2020). Structural basis of self-assembly in the lipid-binding domain of mycobacterial polar growth factor Wag31. IUCrJ, 7(Pt 4), 767-776.

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