jbscreen 5 8  (Jena Bioscience)


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    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, 2021-07
    93/100 stars

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    Related Articles

    Crystallization Assay:

    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: Crystal structure of red chlorophyll catabolite reductase: enlargement of the ferredoxin-dependent bilin reductase family.
    Article Snippet: The key steps in the degradation pathway of chlorophylls are the ring-opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by red chlorophyll catabolite reductase (RCCR). .. The key steps in the degradation pathway of chlorophylls are the ring-opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by red chlorophyll catabolite reductase (RCCR). ..

    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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    80
    Jena Bioscience 2 oh datp
    MTH1 is the target of SCH51344 a , Representation of the chemical proteomic workflow. b , Sructures of SCH51344 ( 1 ) and the probe used for affinity purification ( 2 ). c , Results from MS-based proteomic affinity purification experiment using SAINT and competition analysis. Data shown are based on two independent experiments for each condition (n = 2/condition), and each replicate was analysed in two technical replicates. d , ITC data for MTH1 with SCH51344. The measured K d was 49 nM (n = 1). e , SCH51344 inhibits hydrolysis of the MTH1 substrates dGTP, 8-oxo-dGTP, and <t>2-OH-dATP,</t> respectively. Data are shown for two technical replicates ± SEM and representative for at least duplicate experiments (n ≥ 2). f , Silencing of MTH1 by siRNA impairs colony formation of KRAS-positive SW480 (top) and DLD1 (bottom) cells. Data shown as mean ± SEM and images are representative for triplicate experiments (n = 3) (P
    2 Oh Datp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 80/100, 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:

    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

    MTH1 is the target of SCH51344 a , Representation of the chemical proteomic workflow. b , Sructures of SCH51344 ( 1 ) and the probe used for affinity purification ( 2 ). c , Results from MS-based proteomic affinity purification experiment using SAINT and competition analysis. Data shown are based on two independent experiments for each condition (n = 2/condition), and each replicate was analysed in two technical replicates. d , ITC data for MTH1 with SCH51344. The measured K d was 49 nM (n = 1). e , SCH51344 inhibits hydrolysis of the MTH1 substrates dGTP, 8-oxo-dGTP, and 2-OH-dATP, respectively. Data are shown for two technical replicates ± SEM and representative for at least duplicate experiments (n ≥ 2). f , Silencing of MTH1 by siRNA impairs colony formation of KRAS-positive SW480 (top) and DLD1 (bottom) cells. Data shown as mean ± SEM and images are representative for triplicate experiments (n = 3) (P

    Journal: Nature

    Article Title: Stereospecific targeting of MTH1 by (S)-crizotinib as anticancer strategy

    doi: 10.1038/nature13194

    Figure Lengend Snippet: MTH1 is the target of SCH51344 a , Representation of the chemical proteomic workflow. b , Sructures of SCH51344 ( 1 ) and the probe used for affinity purification ( 2 ). c , Results from MS-based proteomic affinity purification experiment using SAINT and competition analysis. Data shown are based on two independent experiments for each condition (n = 2/condition), and each replicate was analysed in two technical replicates. d , ITC data for MTH1 with SCH51344. The measured K d was 49 nM (n = 1). e , SCH51344 inhibits hydrolysis of the MTH1 substrates dGTP, 8-oxo-dGTP, and 2-OH-dATP, respectively. Data are shown for two technical replicates ± SEM and representative for at least duplicate experiments (n ≥ 2). f , Silencing of MTH1 by siRNA impairs colony formation of KRAS-positive SW480 (top) and DLD1 (bottom) cells. Data shown as mean ± SEM and images are representative for triplicate experiments (n = 3) (P

    Article Snippet: After addition of the substrate dGTP (Fermentas, final concentration 100 μM), 8-oxo-dGTP (TriLink Biotechnologies, final concentration 13.2 μM), or 2-OH-dATP (Jena Bioscience, final concentration 8.3 μM) the generation of pyrophosphate (PPi) as a result of nucleotide triphosphate hydrolysis by MTH1 was monitored over a time course of 15 min using the PPiLight Inorganic Pyrophosphate Assay kit (Lonza Rockland).

    Techniques: Affinity Purification, Mass Spectrometry