Jbscreen classic 1 10

Manufactured by Jena Biosciences

Sourced in United States

The JBScreen Classic 1–10 is a collection of ten pre-formulated screening solutions designed for the crystallization of macromolecules, such as proteins and nucleic acids. Each solution contains a unique combination of precipitants, buffers, and additives to promote the formation of high-quality crystals. The JBScreen Classic 1–10 is a tool used in the initial screening stage of the crystallization process.

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Lab products found in correlation

Crystalquick plates, by Greiner (3 mentions) Jbscreen membrane 1 3, by Jena Biosciences (3 mentions) Pi peg screen hts, by Jena Biosciences (2 mentions) Easyxtal plates, by Qiagen (2 mentions) Pact suite, by Qiagen (1 mentions) Jcsg suite, by Qiagen (1 mentions) Amicon ultra 4, by Merck Group (1 mentions)

5 protocols using jbscreen classic 1 10

Crystallization of Membrane Proteins

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Initial crystallization screens were performed by the sitting-drop vapour-diffusion technique (96-well Crystal Quick plates, Greiner Bio-One) using a nanodispenser robot (Gryphon, Art Robbins). Screening over a broad variety of crystallization conditions (Crystallization Basic Kit for Membrane Proteins, Crystallization Low Ionic Strength Kit for Proteins and Crystallization Basic Kit for Proteins from Sigma–Aldrich; Pi-PEG Screen HTS, JBScreen Classic 1–10 and JBScreen Membrane 1–3 from Jena Bioscience) gave the first hits (microcrystalline precipitant) for crystallization.
The first microcrystals were obtained by the hanging-drop vapour-diffusion technique (15-well EasyXtal 10 × 15 plates, Qiagen) using 10% PEG 4000, 15 mM MgCl₂, 25 mM Tris–HCl pH 7.5 at 291 K as the crystallization condition (Fig. 2 ▶a). The final crystallization condition for the growth of single crystals suitable for diffraction measurements was 10% PEG 4000, 1 mM Na₆[TeW₆O₂₄]·22H₂O, 25 mM Tris–HCl pH 7.5 at 291 K using 1 µl protein solution (10 mg ml⁻¹) and 0.5 µl reservoir solution in the hanging drop and 500 µl solution in the reservoir (Fig. 2 ▶b). The first crystals appeared after 1–2 d and crystal growth came to a stop after approximately 5 d.

Mauracher S.G., Molitor C., Al-Oweini R., Kortz U, & Rompel A. (2014). Crystallization and preliminary X-ray crystallographic analysis of latent isoform PPO4 mushroom (Agaricus bisporus) tyrosinase. Acta Crystallographica. Section F, Structural Biology Communications, 70(Pt 2), 263-266.

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Crystallization Screening for Wildtype MdPPO1

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Initial screening for suitable crystallization conditions for wild-type MdPPO1 was performed by the sitting-drop vapour-diffusion method using a nanodispenser robot (Gryphon, Art Robbins) and 96-well Crystal Quick plates (Greiner Bio-One). A wide range of crystallization conditions were screened by using a variety of commercially available screening kits (JBScreen Classic 1–10, JBScreen Membrane 1–3 and Pi-PEG Screen HTS from Jena Bioscience). The screening procedure yielded some promising hits, which were further optimized manually by applying the hanging-drop vapour-diffusion technique using 15-well EasyXtal plates (Qiagen). Single crystals of wild-type MdPPO1 and of the mutants MdPPO1-Ala239Thr and MdPPO1-Phe259Ala (Fig. 3 ▸) were grown at 20°C by mixing 1 µl protein solution (5–10 mg ml⁻¹) with 2 µl reservoir solution (50 mM Tris–HCl pH 7.0, 19–21% PEG 3350). Crystals usually appeared after 10–15 d. Crystallization information is summarized in Table 2 ▸. Crystallization trials of the mutants MdPPO1-Leu243Arg and MdPPO1-Glu234Ala applying the above-described methods yielded only low-quality crystals which were not suitable for adequate data collection (Fig. 3 ▸).

Kampatsikas I., Bijelic A., Pretzler M, & Rompel A. (2017). In crystallo activity tests with latent apple tyrosinase and two mutants reveal the importance of the mutated sites for polyphenol oxidase activity. Acta Crystallographica. Section F, Structural Biology Communications, 73(Pt 8), 491-499.

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Crystallization Protocol for Protein Structure

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Initial screening for crystallization was carried out by the sitting-drop vapour-diffusion method (96-well CrystalQuick plates, Greiner Bio-One) employing a nanodispenser robot (Gryphon, Art Robbins). Initial hits were obtained by screening over a broad variety of commercially available screening kits (JBScreen Classic 1–10 and JBScreen Membrane 1–3 from Jena Bioscience) mixing the protein solution with the reservoir solution in a 1:2 ratio. Further optimization of the crystallization conditions was performed manually in 15-well EasyXtal plates (Qiagen) applying the hanging-drop vapour-diffusion method at 293 K. Single crystals suitable for diffraction measurements were obtained after 2–3 d by mixing 1 µl protein solution (10 mg ml⁻¹) with 0.5 µl reservoir solution and equilibrating against 500 µl reservoir solution consisting of 30% PEG 5000 MME (MME, monomethyl ether), 200 mM ammonium sulfate, 100 mM MES pH 6.5 (Fig. 1 ▶). The crystals stopped growing after approximately 6 d.

Zekiri F., Bijelic A., Molitor C, & Rompel A. (2014). Crystallization and preliminary X-ray crystallographic analysis of polyphenol oxidase from Juglans regia (jrPPO1). Acta Crystallographica. Section F, Structural Biology Communications, 70(Pt 6), 832-834.

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Crystallization of CtPFD Protein

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CtPFD (15 or 7.5 mg/mL) was mixed with 250 kinds of reservoir solutions (JBScreen Classic1-10, Jena Bioscience) and crystals were grown by the vapor diffusion method. The CtPFD crystals were obtained when CtPFD was mixed with 200 mM ammonium di-hydrogen phosphate. The crystals were soaked in a reservoir solution supplemented with 20% (w/v) PEG 4000, and flash-cooled in a nitrogen-gas stream at 95 K. The X-ray diffraction data were collected on beamline BL1A at the Photon Factory.

Morita K., Yamamoto Y.Y., Hori A., Obata T., Uno Y., Shinohara K., Noguchi K., Noi K., Ogura T., Ishii K., Kato K., Kikumoto M., Arranz R., Valpuesta J.M, & Yohda M. (2018). Expression, Functional Characterization, and Preliminary Crystallization of the Cochaperone Prefoldin from the Thermophilic Fungus Chaetomium thermophilum. International Journal of Molecular Sciences, 19(8), 2452.

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Optimized Crystallization of VLRC Protein

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Prior to crystallization trials, VLRC was concentrated to a final concentration of 10 mg ml⁻¹ in a buffer containing 10 mM Tris-HCl (pH 8.0) and 50 mM NaCl. Concentration was carried out using a Millipore centrifugal filter device (Amicon Ultra-4, 10 kDa cutoff; Millipore, USA). Screening for crystallization was performed using Wizard Screens I and II (Emerald Biosciences, USA), JBScreen Classic 1–10 (Jena Bioscience, Germany), JCSG + suite, PACT suite, and the PEGs and PEGs II suites (Qiagen, Germany) by the sitting-drop vapor diffusion method in 96-well plates (SWISSCI MRC 2 Well, Jena Bioscience, Germany). A drop of 0.1 µl of the sample was mixed with an equal volume of reservoir solution. The mixture was equilibrated against 0.1 ml of reservoir solution at 293 K. Crystals were grown from PEGs suite #89 (0.2 M potassium phosphate, 20% (w/v) PEG3350). Based on this result, an extensive optimization in a 96-well sitting-drop format was carried out. A diffraction-quality crystal was obtained by mixing 0.2 µl protein solution (15 mg ml⁻¹) and 0.2 µl reservoir solution [0.2 M potassium phosphate, 20% (w/v) PEG3350], and then equilibrating the drops against 60 µl of the reservoir solution at 293 K.

Kanda R., Sutoh Y., Kasamatsu J., Maenaka K., Kasahara M, & Ose T. (2014). Crystal Structure of the Lamprey Variable Lymphocyte Receptor C Reveals an Unusual Feature in Its N-Terminal Capping Module. PLoS ONE, 9(1), e85875.

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