jbscreen 5 8  (Jena Bioscience)


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  • 93
    Name:
    JBScreen Classic 1 5
    Description:

    Catalog Number:
    CS-112L
    Price:
    593.0
    Category:
    Crystallography
    Size:
    5 Kits
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    Structured Review

    Jena Bioscience jbscreen 5 8

    https://www.bioz.com/result/jbscreen 5 8/product/Jena Bioscience
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    jbscreen 5 8 - by Bioz Stars, 2021-06
    93/100 stars

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    Related Articles

    Crystallization Assay:

    Article Title: The complex between SOS3 and SOS2 regulatory domain from Arabidopsis thaliana: cloning, expression, purification, crystallization and preliminary X-ray analysis
    Article Snippet: Thus, it was decided to clone and express the truncated SOS3 protein in order to avoid heterogeneity in crystallization experiments. .. Preliminary crystallization conditions were established using JBScreen Classic Kit 1–10 (Jena Biosciences) with the hanging-drop vapour-diffusion method at 293†K. Drops containing equal volumes (1†µl) of protein (10†mg†ml−1 ) and reservoir solution were equilibrated against 500†µl reservoir solution. .. Condition No. B5 [20%( w / v ) PEG 4000, 0.1  M Tris–HCl pH 8.5, 0.2  M lithium sulfate] from JBScreen Classic Kit 2 (PEG 4000-based; Jena Biosciences) produced needle-like crystals in 5 d (see Fig. 3 a ).

    Article Title: High-Resolution Crystal Structure of Chloroplastic Ribose-5-Phosphate Isomerase from Chlamydomonas reinhardtii—An Enzyme Involved in the Photosynthetic Calvin-Benson Cycle
    Article Snippet: Proteins were then analyzed by injection on a Superose 6 increase size exclusion chromatography column in buffer C (20 mM Tris-HCl pH 7.9, 100 mmol/L NaCl). .. Protein Crystallization and Structure Determination Purified CrRPI1 was tested for crystallization on commercial sparse-screening conditions (Qiagen, Hilden Germany) of the Joint Center for Structural Genomics screens [ ] and JBScreen classic 1–8 (Jena Bioscience, Jena, Germany) with a mixture of 50 nL of protein and 50 nL of precipitant solution equilibrated against 30 µL of reservoir solution at 20 °C. ..

    Article Title: The epithelial adhesin 1 (Epa1p) from the human-pathogenic yeast Candida glabrata: structural and functional study of the carbohydrate-binding domain.
    Article Snippet: The yeast Candida glabrata represents the second major cause of clinical candidiasis cases in the world. .. The yeast Candida glabrata represents the second major cause of clinical candidiasis cases in the world. .. The yeast Candida glabrata represents the second major cause of clinical candidiasis cases in the world.

    Article Title: Expression, purification and preliminary crystallographic analysis of the cryptic polo-box domain of Caenorhabditis elegans ZYG-1
    Article Snippet: .. The screening of crystallization conditions was performed at both 277 and 295 K using three commercial crystallization kits: Crystal Screen HT (Hampton Research), Cryo 1 & 2 (Emerald Bio) and JBScreen Classic 1–4 (Jena Bioscience). .. All conditions were dispensed by a Crystal Phoenix Robot (Art Robbins Instruments) into two-well MRC plates (Hampton Research) using protein:mother liquor ratios of 100:100 nl and 200:100 nl.

    Purification:

    Article Title: High-Resolution Crystal Structure of Chloroplastic Ribose-5-Phosphate Isomerase from Chlamydomonas reinhardtii—An Enzyme Involved in the Photosynthetic Calvin-Benson Cycle
    Article Snippet: Proteins were then analyzed by injection on a Superose 6 increase size exclusion chromatography column in buffer C (20 mM Tris-HCl pH 7.9, 100 mmol/L NaCl). .. Protein Crystallization and Structure Determination Purified CrRPI1 was tested for crystallization on commercial sparse-screening conditions (Qiagen, Hilden Germany) of the Joint Center for Structural Genomics screens [ ] and JBScreen classic 1–8 (Jena Bioscience, Jena, Germany) with a mixture of 50 nL of protein and 50 nL of precipitant solution equilibrated against 30 µL of reservoir solution at 20 °C. ..

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  • 93
    Jena Bioscience 8 oxo dgtp
    (A) Ribbon diagram of the Vc MutT X-ray structure with β-strands in firebrick red, α-helices in brown and loops in grey. (B) Homology model of Vc MutT-closed (grey) made from Ec <t>MutT-8-oxo-dGTP-Mn</t> superimposed on Vc MutT (firebrick red). 8-oxo-dGMP and Mn 2+ are modelled from the Ec MutT-8-oxo-dGTP-Mn structure. (C) Hydrogen bonding interactions between 8-oxo-dGMP and Vc MutT (crystal structure in firebrick red and closed homology model in grey). The super imposed As MutT models (closed in dark-grey and open in sky-blue) are also shown. Residues involved in Mn 2+ coordination and residues promoting conformational stabilization to the enzymes structure are indicated. (D) Hydrogen bonds between the Vc MutT-closed model and 8-oxo-dGMP. Electrostatic surface of the homology model of (E) Vc MutT-closed and (F) As MutT-closed with important residue differences highlighted. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    8 Oxo Dgtp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Jena Bioscience nucleotide analogue maba adp
    MANF inhibits nucleotide exchange and ATP-induced substrate release from BiP. a Representative plot of fluorescence against time of pre-formed complexes of <t>MABA-ADP</t> and BiP NBD (1.25 µM) challenged at t = 0 with buffer solution containing ATP (125 µM) and MANF or its SAP domain (200 µM). b Bar diagram of MABA-ADP release rates from BiP NBD in the presence of MANF, the isolated SAP or SAPLIP domain or the indicated mutant forms of MANF. Bars represent mean values ± SD from three to five independent experiments (**** P
    Nucleotide Analogue Maba Adp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Jena Bioscience chitinase a
    Purification of <t>chitinase</t> A expressed from E. coli M15 cells. ( a ) Elution profile of recombinant chitinase A obtained from an ÄKTA purifier system with a Superdex 200 HR 10/30 (1.0 × 30 cm) gel-filtration column. The running buffer
    Chitinase A, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    (A) Ribbon diagram of the Vc MutT X-ray structure with β-strands in firebrick red, α-helices in brown and loops in grey. (B) Homology model of Vc MutT-closed (grey) made from Ec MutT-8-oxo-dGTP-Mn superimposed on Vc MutT (firebrick red). 8-oxo-dGMP and Mn 2+ are modelled from the Ec MutT-8-oxo-dGTP-Mn structure. (C) Hydrogen bonding interactions between 8-oxo-dGMP and Vc MutT (crystal structure in firebrick red and closed homology model in grey). The super imposed As MutT models (closed in dark-grey and open in sky-blue) are also shown. Residues involved in Mn 2+ coordination and residues promoting conformational stabilization to the enzymes structure are indicated. (D) Hydrogen bonds between the Vc MutT-closed model and 8-oxo-dGMP. Electrostatic surface of the homology model of (E) Vc MutT-closed and (F) As MutT-closed with important residue differences highlighted. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: FEBS Open Bio

    Article Title: MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability

    doi: 10.1016/j.fob.2015.01.006

    Figure Lengend Snippet: (A) Ribbon diagram of the Vc MutT X-ray structure with β-strands in firebrick red, α-helices in brown and loops in grey. (B) Homology model of Vc MutT-closed (grey) made from Ec MutT-8-oxo-dGTP-Mn superimposed on Vc MutT (firebrick red). 8-oxo-dGMP and Mn 2+ are modelled from the Ec MutT-8-oxo-dGTP-Mn structure. (C) Hydrogen bonding interactions between 8-oxo-dGMP and Vc MutT (crystal structure in firebrick red and closed homology model in grey). The super imposed As MutT models (closed in dark-grey and open in sky-blue) are also shown. Residues involved in Mn 2+ coordination and residues promoting conformational stabilization to the enzymes structure are indicated. (D) Hydrogen bonds between the Vc MutT-closed model and 8-oxo-dGMP. Electrostatic surface of the homology model of (E) Vc MutT-closed and (F) As MutT-closed with important residue differences highlighted. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: A central question in the field is how MutT enzymes favour the recognition of 8-oxo-dGTP over dGTP?

    Techniques:

    Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b Graph shows time-dependent changes in the products of insertion (pink and purple for 8-oxodGTP and dGTP insertions, respectively) and ligation (cyan and blue for ligation following insertion of 8-oxodGTP and dGTP, respectively). The data represent the average of four independent experiments ± SD. Corresponding uncropped gel image and presentation of the data in line graph format are shown in Supplementary Fig. 2

    Journal: Nature Communications

    Article Title: Pol μ dGTP mismatch insertion opposite T coupled with ligation reveals promutagenic DNA repair intermediate

    doi: 10.1038/s41467-018-06700-5

    Figure Lengend Snippet: Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b Graph shows time-dependent changes in the products of insertion (pink and purple for 8-oxodGTP and dGTP insertions, respectively) and ligation (cyan and blue for ligation following insertion of 8-oxodGTP and dGTP, respectively). The data represent the average of four independent experiments ± SD. Corresponding uncropped gel image and presentation of the data in line graph format are shown in Supplementary Fig. 2

    Article Snippet: Briefly, the reaction mixture (10 μl in final volume) included 50 mM Tris(HCl), pH 7.5, 100 mM KCl, 10 mM MgCl2 , 1 mM ATP, 100 μg ml−1 BSA, 10% glycerol, 1 mM DTT, and 200 μM of 8-oxodGTP (Jena Bioscience), dGTP or dATP (NEB), 300 nM DNA substrate, and 100 nM enzyme mixture.

    Techniques: Ligation

    MANF inhibits nucleotide exchange and ATP-induced substrate release from BiP. a Representative plot of fluorescence against time of pre-formed complexes of MABA-ADP and BiP NBD (1.25 µM) challenged at t = 0 with buffer solution containing ATP (125 µM) and MANF or its SAP domain (200 µM). b Bar diagram of MABA-ADP release rates from BiP NBD in the presence of MANF, the isolated SAP or SAPLIP domain or the indicated mutant forms of MANF. Bars represent mean values ± SD from three to five independent experiments (**** P

    Journal: Nature Communications

    Article Title: MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP

    doi: 10.1038/s41467-019-08450-4

    Figure Lengend Snippet: MANF inhibits nucleotide exchange and ATP-induced substrate release from BiP. a Representative plot of fluorescence against time of pre-formed complexes of MABA-ADP and BiP NBD (1.25 µM) challenged at t = 0 with buffer solution containing ATP (125 µM) and MANF or its SAP domain (200 µM). b Bar diagram of MABA-ADP release rates from BiP NBD in the presence of MANF, the isolated SAP or SAPLIP domain or the indicated mutant forms of MANF. Bars represent mean values ± SD from three to five independent experiments (**** P

    Article Snippet: Fluorescence measurement Nucleotide release kinetics of the fluorescent nucleotide analogue MABA-ADP (Jena Bioscience, cat. # NU-893-MNT) and nucleotide binding of MABA-ATP (Jena Bioscience, cat. # NU-806-MNT) were performed in a Perkin Elmer LS55 fluorescence spectrometer instrument (excitation 360 nm, emission 420 nm).

    Techniques: Fluorescence, Isolation, Mutagenesis

    Purification of chitinase A expressed from E. coli M15 cells. ( a ) Elution profile of recombinant chitinase A obtained from an ÄKTA purifier system with a Superdex 200 HR 10/30 (1.0 × 30 cm) gel-filtration column. The running buffer

    Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

    Article Title: Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae

    doi: 10.1107/S1744309105027831

    Figure Lengend Snippet: Purification of chitinase A expressed from E. coli M15 cells. ( a ) Elution profile of recombinant chitinase A obtained from an ÄKTA purifier system with a Superdex 200 HR 10/30 (1.0 × 30 cm) gel-filtration column. The running buffer

    Article Snippet: For each crystallization drop, 0.5 µl chitinase A (10 mg ml−1 in 20 m M Tris–HCl buffer pH 8.0 containing 150 m M NaCl) was added to 0.5 µl of each precipitant from Crystal Screen (Hampton Research) and JB Screen HTS I and HTS II (Jena Bioscience GmbH, Jena, Germany) without mixing.

    Techniques: Purification, Recombinant, Filtration

    A crystal of recombinant chitinase A (dimensions 1100 × 400 × 100 µm) obtained from a hanging-drop vapour-diffusion setup using 0.1 M sodium acetate pH 4.6 containing 10%( v / v ) PEG 400 and 0.125 M CaCl 2 .

    Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

    Article Title: Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae

    doi: 10.1107/S1744309105027831

    Figure Lengend Snippet: A crystal of recombinant chitinase A (dimensions 1100 × 400 × 100 µm) obtained from a hanging-drop vapour-diffusion setup using 0.1 M sodium acetate pH 4.6 containing 10%( v / v ) PEG 400 and 0.125 M CaCl 2 .

    Article Snippet: For each crystallization drop, 0.5 µl chitinase A (10 mg ml−1 in 20 m M Tris–HCl buffer pH 8.0 containing 150 m M NaCl) was added to 0.5 µl of each precipitant from Crystal Screen (Hampton Research) and JB Screen HTS I and HTS II (Jena Bioscience GmbH, Jena, Germany) without mixing.

    Techniques: Recombinant, Diffusion-based Assay