nextal classics suite  (Qiagen)


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  • 99
    Name:
    NeXtal DWBlock Classics L Suite
    Description:
    For manual or automated setup of protein crystallization screening conditions Kit contents Piercable deep well block containing 96 x 1 5 ml Classics Lite Suite solution piercing tool adhesive foil Benefits 1 5 ml solution of each Screening Suite condition in a 96 well format For manual or automated setup in microplates Heat sealed pierceable foil ensures optimal storage and shipping Maximized reproducibility through online access to production repor
    Catalog Number:
    130902
    Price:
    359
    Category:
    NeXtal DWBlock Suites
    Buy from Supplier


    Structured Review

    Qiagen nextal classics suite
    NeXtal DWBlock Classics L Suite
    For manual or automated setup of protein crystallization screening conditions Kit contents Piercable deep well block containing 96 x 1 5 ml Classics Lite Suite solution piercing tool adhesive foil Benefits 1 5 ml solution of each Screening Suite condition in a 96 well format For manual or automated setup in microplates Heat sealed pierceable foil ensures optimal storage and shipping Maximized reproducibility through online access to production repor
    https://www.bioz.com/result/nextal classics suite/product/Qiagen
    Average 99 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    nextal classics suite - by Bioz Stars, 2020-04
    99/100 stars

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    Related Articles

    Chromatography:

    Article Title: An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase
    Article Snippet: The protein was then exchanged into 10 mM HEPES, pH 7.5, 0.1 M KCl, 5 mM DTT by gel-filtration chromatography and concentrated to 10 mg/mL. .. The filtered protein was screened for suitable crystallization conditions using the NeXtal Classics Suite from Qiagen (Germantown, MD) by the hanging drop vapor diffusion method in the anaerobic chamber at RT.

    Spectrophotometry:

    Article Title: Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum
    Article Snippet: The absorption was measured using a Nanodrop spectrophotometer (Thermo Fisher Scientific, Waltham, Massachusetts, USA). .. Crystallization screening of the native protein was performed with NeXtal Classics Suite, NeXtal Classics Lite Suite, NeXtal JCSG+ Suite and NeXtal JCSG Core Suite I–IV (Qiagen), giving a total of 672 conditions, using the sitting-drop method by mixing 1 µl protein solution (approximately 1 mg ml−1 in 20 m M Tris–HCl pH 8.0 and 200 m M NaCl) with 1 µl reservoir buffer and equilibrating against 100 µl reservoir buffer at 293 K. The crystals of native protein that were most suitable for further diffraction experiments were grown with 0.2 M potassium/sodium tartrate, 0.1 M trisodium citrate pH 5.6 and 1 M ammonium sulfate (Fig. 1 ).

    Purification:

    Article Title: Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum
    Article Snippet: The purified protein was concentrated to approximately 1 mg ml−1 using an Amicon Ultra-15 ultrafiltration device (Millipore, Billerica, Massachusetts, USA) for crystallization. .. Crystallization screening of the native protein was performed with NeXtal Classics Suite, NeXtal Classics Lite Suite, NeXtal JCSG+ Suite and NeXtal JCSG Core Suite I–IV (Qiagen), giving a total of 672 conditions, using the sitting-drop method by mixing 1 µl protein solution (approximately 1 mg ml−1 in 20 m M Tris–HCl pH 8.0 and 200 m M NaCl) with 1 µl reservoir buffer and equilibrating against 100 µl reservoir buffer at 293 K. The crystals of native protein that were most suitable for further diffraction experiments were grown with 0.2 M potassium/sodium tartrate, 0.1 M trisodium citrate pH 5.6 and 1 M ammonium sulfate (Fig. 1 ).

    Concentration Assay:

    Article Title: An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase
    Article Snippet: Following concentration of the reconstituted (RCN) protein, it was loaded onto a prepacked HiPrep 16/60 Sephacryl S-200 HR column equilibrated in 50 mM HEPES, pH 7.5, 0.1 M KCl, 10 mM DTT and 10% glycerol that was connected to an ÅKTA chromatography system housed in a Coy (Grass Lake, MI) anaerobic glove box. .. The filtered protein was screened for suitable crystallization conditions using the NeXtal Classics Suite from Qiagen (Germantown, MD) by the hanging drop vapor diffusion method in the anaerobic chamber at RT.

    Diffusion-based Assay:

    Article Title: An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase
    Article Snippet: .. The filtered protein was screened for suitable crystallization conditions using the NeXtal Classics Suite from Qiagen (Germantown, MD) by the hanging drop vapor diffusion method in the anaerobic chamber at RT. ..

    Protein Concentration:

    Article Title: Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum
    Article Snippet: The protein concentration was determined by monitoring the absorption at a wavelength of 280 nm with a molar extinction coefficient of 85 760 M −1 , as determined from the amino-acid sequence. .. Crystallization screening of the native protein was performed with NeXtal Classics Suite, NeXtal Classics Lite Suite, NeXtal JCSG+ Suite and NeXtal JCSG Core Suite I–IV (Qiagen), giving a total of 672 conditions, using the sitting-drop method by mixing 1 µl protein solution (approximately 1 mg ml−1 in 20 m M Tris–HCl pH 8.0 and 200 m M NaCl) with 1 µl reservoir buffer and equilibrating against 100 µl reservoir buffer at 293 K. The crystals of native protein that were most suitable for further diffraction experiments were grown with 0.2 M potassium/sodium tartrate, 0.1 M trisodium citrate pH 5.6 and 1 M ammonium sulfate (Fig. 1 ).

    Sequencing:

    Article Title: Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum
    Article Snippet: The protein concentration was determined by monitoring the absorption at a wavelength of 280 nm with a molar extinction coefficient of 85 760 M −1 , as determined from the amino-acid sequence. .. Crystallization screening of the native protein was performed with NeXtal Classics Suite, NeXtal Classics Lite Suite, NeXtal JCSG+ Suite and NeXtal JCSG Core Suite I–IV (Qiagen), giving a total of 672 conditions, using the sitting-drop method by mixing 1 µl protein solution (approximately 1 mg ml−1 in 20 m M Tris–HCl pH 8.0 and 200 m M NaCl) with 1 µl reservoir buffer and equilibrating against 100 µl reservoir buffer at 293 K. The crystals of native protein that were most suitable for further diffraction experiments were grown with 0.2 M potassium/sodium tartrate, 0.1 M trisodium citrate pH 5.6 and 1 M ammonium sulfate (Fig. 1 ).

    Crystallization Assay:

    Article Title: Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum
    Article Snippet: .. Crystallization screening of the native protein was performed with NeXtal Classics Suite, NeXtal Classics Lite Suite, NeXtal JCSG+ Suite and NeXtal JCSG Core Suite I–IV (Qiagen), giving a total of 672 conditions, using the sitting-drop method by mixing 1 µl protein solution (approximately 1 mg ml−1 in 20 m M Tris–HCl pH 8.0 and 200 m M NaCl) with 1 µl reservoir buffer and equilibrating against 100 µl reservoir buffer at 293 K. The crystals of native protein that were most suitable for further diffraction experiments were grown with 0.2 M potassium/sodium tartrate, 0.1 M trisodium citrate pH 5.6 and 1 M ammonium sulfate (Fig. 1 ). .. The crystallization conditions for the SeMet-derivative protein were optimized based on the conditions that gave crystals of native protein using StockOptions Salt (Hampton Research, Aliso Viejo, California, USA), in which individual salt candidates were mixed with the original solution in a 1:5 ratio (salt:original solution).

    Article Title: An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase
    Article Snippet: .. The filtered protein was screened for suitable crystallization conditions using the NeXtal Classics Suite from Qiagen (Germantown, MD) by the hanging drop vapor diffusion method in the anaerobic chamber at RT. ..

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