Saturn 944 hg

Manufactured by Rigaku

The Saturn 944 HG is an X-ray diffraction system designed for high-resolution structural analysis. It features a high-brilliance X-ray source and a large area detector to collect diffraction data efficiently. The system is capable of performing various X-ray diffraction techniques, including single-crystal and powder diffraction analysis.

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Fr e superbright, by Rigaku (1 mentions) Micromax 003, by Rigaku (1 mentions) Micromax 007hf, by Rigaku (1 mentions)

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4 protocols using saturn 944 hg

Protein Crystallization and Structure Determination

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Crystals of apo-PPZ1_cat were obtained using hanging drop vapor diffusion in 1.8 M ammonium citrate tribasic (pH 7.0) in a 2:1 protein/crystallization condition ratio. To generate PPZ1_cat-MC crystals, PPZ1_cat was first incubated with MC at a 1:1 molar ratio for 15 min before crystallization using hanging drop vapor diffusion in 0.06 M citric acid (pH 4.1) plus 16% (wt/vol) polyethylene glycol (PEG) 3350. For data collection, crystals were first cryo-protected with 30% glycerol in mother liquor (PPZ1_cat) or 3.4 M Na-malonate (pH 4.0) (PPZ1_cat-MC) and then flash-frozen in liquid nitrogen. X-ray data were collected in house at 100 K using a Rigaku FR-E+ Superbright rotating copper anode X-ray generator with a Saturn 944+ HG charge-coupled device (CCD) detector (Brown University Structural Biology Facility). The data were phased using molecular replacement (Phaser as implemented in PHENIX [39 (link)]) using PP1 (PDB no. 4MOV [19 (link)]) as the search model. Clear electron density of MC could be observed bound to the active site. The initial models were built using Phenix.AutoBuild (40 (link)) followed by iterative rounds of refinement in PHENIX and manual building using Coot (41 (link)).

Chen E., Choy M.S., Petrényi K., Kónya Z., Erdődi F., Dombrádi V., Peti W, & Page R. (2016). Molecular Insights into the Fungus-Specific Serine/Threonine Protein Phosphatase Z1 in Candida albicans. mBio, 7(4), e00872-16.

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Structural Determination of CRISPR HNH Domain

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Following TEV cleavage of the His₆-tag, HNH was subsequently purified by HiPrep 16/60 Sephacryl 100 S-100 HR gel filtration chromatography. Crystals were obtained with sitting drop vapor diffusion at room temperature with 48 mg/mL HNH 1:1 with the Molecular Dimensions Morpheus I Screen condition E4 (0.1 M mixture of [imidazole and MES] pH 6.5, 25% (v/v) mixture of [2-methyl-2,4-pentanediol, PEG1000, and PEG3350], and 0.3 M mixture of [diethylene glycol, triethylene glycol, tetraethylene glycol, and pentaethlyene glycol]). Diffraction data were collected on a Rigaku MicroMax-003i sealed tube X-ray generator with a Saturn 944 HG CCD detector and processed and scaled using XDS^{64 (link)} and Aimless in the CCP4 program suite.^{65 (link)} The HNH domain from full-length S. pyogenes Cas9 was used for molecular replacement (PDB: 4UN3)^{5 (link)} with Phaser in the PHENIX software package.^{66 (link)} Iterative rounds of manual building in Coot^{67 (link)} and refinement in PHENIX yielded the final HNH domain structure.

East K.W., Newton J.C., Morzan U.N., Narkhede Y., Acharya A., Skeens E., Jogl G., Batista V.S., Palermo G, & Lisi G.P. (2020). Allosteric Motions of the CRISPR-Cas9 HNH Nuclease Probed by NMR and Molecular Dynamics. Journal of the American Chemical Society, 142(3), 1348-1358.

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Structural Analysis of SETD2-H3K36M Complexes

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X-ray diffraction data set on a SETD2-SAM-H3K36M complex crystal was collected using a Saturn944HG CCD mounted on a Rigaku Micromax-003 X-ray generator. X-ray diffraction data set on a SETD2-SAH-H3K36M complex crystal was collected at the Advanced Photon Source beamline NE-CAT 24-ID-E using an ADSC Q315r detector. The diffraction images were processed and scaled with the HKL-2000 package29 .

Zhang Y., Shan C.M., Wang J., Bao K., Tong L, & Jia S. (2017). Molecular basis for the role of oncogenic histone mutations in modulating H3K36 methylation. Scientific Reports, 7, 43906.

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Crystallization of A3A(E72A/C171A)-DNA Complex

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Crystals of the A3A(E72A/C171A)–DNA complex were grown by hanging-drop vapour-diffusion method over a reservoir of 100 mM MOPS (pH 6.5), 50 mM MgCl₂, 50 mM CaCl₂, 23% polyethylene glycol 3,350 and 15% 2-methyl-2,4-pentanediol. Drops were formed by mixing 1 μl of A3A(E72A/C171A)–DNA solution (∼20 mg ml^−l of protein concentration) and 1 μl of reservoir solution, with equilibration over the reservoir at 20 °C. Micro-seeding was performed using a cat whisker and larger crystals suitable for X-ray diffraction were obtained. Crystals were flash-frozen directly in the cryogenic stream. Diffraction data were collected using an in-house X-ray source MicroMax-007 HF (Rigaku) with a copper anode at a wavelength of 1.54178 Å and a Saturn 944 HG (Rigaku) detector. The space group of the crystals was I222 with unit cell dimensions of a=56.6 Å, b=72.7 Å, c=115.0 Å (Table 1). The collected intensities were indexed, integrated, corrected for absorption and scaled using HKL2000 (ref. 62 ).

Kouno T., Silvas T.V., Hilbert B.J., Shandilya S.M., Bohn M.F., Kelch B.A., Royer W.E., Somasundaran M., Kurt Yilmaz N., Matsuo H, & Schiffer C.A. (2017). Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity. Nature Communications, 8, 15024.

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