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grna chemical synthesis  (GenScript corporation)

 
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    GenScript corporation grna chemical synthesis
    The length of DNA target affects NADase activation. ( A ) SEC experiments assaying the binding ability of CrtSPARTA 1–421 <t>to</t> <t>gDNA</t> and tDNA of different lengths (5, 10, 15, and 21 nt). The peak fraction is analyzed by SDS–PAGE and TBE–urea PAGE. ( B ) The schematic representation of the gDNA and tDNA of different lengths. ( C ) NADase activity assays with 21-nt gDNA or <t>gRNA</t> and different lengths of tDNA. Data are shown as mean ± standard deviation ( n = 3 independent experiments).
    Grna Chemical Synthesis, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/grna chemical synthesis/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    grna chemical synthesis - by Bioz Stars, 2026-06
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    1) Product Images from "Structural basis of ssDNA-guided NADase activation of prokaryotic SPARTA system"

    Article Title: Structural basis of ssDNA-guided NADase activation of prokaryotic SPARTA system

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkaf110

    The length of DNA target affects NADase activation. ( A ) SEC experiments assaying the binding ability of CrtSPARTA 1–421 to gDNA and tDNA of different lengths (5, 10, 15, and 21 nt). The peak fraction is analyzed by SDS–PAGE and TBE–urea PAGE. ( B ) The schematic representation of the gDNA and tDNA of different lengths. ( C ) NADase activity assays with 21-nt gDNA or gRNA and different lengths of tDNA. Data are shown as mean ± standard deviation ( n = 3 independent experiments).
    Figure Legend Snippet: The length of DNA target affects NADase activation. ( A ) SEC experiments assaying the binding ability of CrtSPARTA 1–421 to gDNA and tDNA of different lengths (5, 10, 15, and 21 nt). The peak fraction is analyzed by SDS–PAGE and TBE–urea PAGE. ( B ) The schematic representation of the gDNA and tDNA of different lengths. ( C ) NADase activity assays with 21-nt gDNA or gRNA and different lengths of tDNA. Data are shown as mean ± standard deviation ( n = 3 independent experiments).

    Techniques Used: Activation Assay, Binding Assay, SDS Page, Activity Assay, Standard Deviation

    Overall structure of CrtSPARTA 1–421 in complex with gDNA and 21-nt tDNA. ( A ) Schematic representation of 5′-P gDNA and tDNA oligonucleotides used for crystallization. ( B ) The overall structure of gDNA and 21-nt tDNA-bound CrtSPARTA 1–421 complex. ( C ) Schematic representation of the intermolecular contacts between SPARTA and guide–target duplex in the complex structure. The base, backbone sugar, and phosphate group of the gDNA and tDNA are shown as rectangles, pentagons, and circles, respectively. Protein residues are color-coded by their respective domains. ( D ) Electron density map of the gDNA–tDNA duplex. The 2mFo-Fc electron density map of the gDNA–tDNA duplex is shown as a mesh (contoured at 1.0σ). ( E ) Structure of the gDNA–tDNA duplex. ( F ) The gDNA–tDNA duplex binds in the positively charged channel of the CrtSPARTA. ( G ) Detailed interactions between the 3′-end nucleotides (A1′–T0′) of tDNA and the MID binding pocket of SPARTA. ( H ) Detailed interactions between the 5′-end nucleotides (T1–G2) of gDNA and the MID domain of SPARTA. The surface representation of CrtSPARTA reveals distinct spatial localization of the gDNA–tDNA duplex ( I ) and gRNA–tDNA duplex ( J ). ( K ) The superposition of the gDNA–tDNA duplex with the gRNA–tDNA duplex in CrtSPARTA complexes reveals distinct models for nucleic acid recognition.
    Figure Legend Snippet: Overall structure of CrtSPARTA 1–421 in complex with gDNA and 21-nt tDNA. ( A ) Schematic representation of 5′-P gDNA and tDNA oligonucleotides used for crystallization. ( B ) The overall structure of gDNA and 21-nt tDNA-bound CrtSPARTA 1–421 complex. ( C ) Schematic representation of the intermolecular contacts between SPARTA and guide–target duplex in the complex structure. The base, backbone sugar, and phosphate group of the gDNA and tDNA are shown as rectangles, pentagons, and circles, respectively. Protein residues are color-coded by their respective domains. ( D ) Electron density map of the gDNA–tDNA duplex. The 2mFo-Fc electron density map of the gDNA–tDNA duplex is shown as a mesh (contoured at 1.0σ). ( E ) Structure of the gDNA–tDNA duplex. ( F ) The gDNA–tDNA duplex binds in the positively charged channel of the CrtSPARTA. ( G ) Detailed interactions between the 3′-end nucleotides (A1′–T0′) of tDNA and the MID binding pocket of SPARTA. ( H ) Detailed interactions between the 5′-end nucleotides (T1–G2) of gDNA and the MID domain of SPARTA. The surface representation of CrtSPARTA reveals distinct spatial localization of the gDNA–tDNA duplex ( I ) and gRNA–tDNA duplex ( J ). ( K ) The superposition of the gDNA–tDNA duplex with the gRNA–tDNA duplex in CrtSPARTA complexes reveals distinct models for nucleic acid recognition.

    Techniques Used: Crystallization Assay, Binding Assay

    Overall architecture of CrtSPARTA 1–421 in complex with gDNA and 16-nt tDNA. ( A ) The sequences of 5′-P gDNA and 16-nt tDNA were used for crystallization. ( B ) The overall structure of gDNA and 16-nt tDNA-bound CrtSPARTA 1–421 complex. ( C ) Schematic representation of the intermolecular contacts between SPARTA and guide–target duplex in the complex structure. The base, backbone sugar, and phosphate group of the gDNA and tDNA are shown as rectangles, pentagons, and circles, respectively. Protein residues are color-coded by their respective domains. ( D ) Electron density map of the gDNA–tDNA duplex. The 2mFo-Fc electron density map of the gDNA–tDNA duplex is shown as a mesh (contoured at 1.0σ). ( E ) Detailed interactions between the nucleotides G15–A17 of gDNA and the MID and PIWI domains of SPARTA. ( F ) Detailed interactions between the 5′-end nucleotides (C15′–A13′) of tDNA and the MID binding pocket of SPARTA. The surface representation of CrtSPARTA reveals distinct spatial localization of the 15-bp gDNA–tDNA duplex ( G ) and 20-bp gRNA–tDNA duplex ( H ). ( I ) The superposition of the 15-bp gDNA–tDNA duplex with the 20-bp gRNA–tDNA duplex in CrtSPARTA complexes reveals distinct models for nucleic acid recognition.
    Figure Legend Snippet: Overall architecture of CrtSPARTA 1–421 in complex with gDNA and 16-nt tDNA. ( A ) The sequences of 5′-P gDNA and 16-nt tDNA were used for crystallization. ( B ) The overall structure of gDNA and 16-nt tDNA-bound CrtSPARTA 1–421 complex. ( C ) Schematic representation of the intermolecular contacts between SPARTA and guide–target duplex in the complex structure. The base, backbone sugar, and phosphate group of the gDNA and tDNA are shown as rectangles, pentagons, and circles, respectively. Protein residues are color-coded by their respective domains. ( D ) Electron density map of the gDNA–tDNA duplex. The 2mFo-Fc electron density map of the gDNA–tDNA duplex is shown as a mesh (contoured at 1.0σ). ( E ) Detailed interactions between the nucleotides G15–A17 of gDNA and the MID and PIWI domains of SPARTA. ( F ) Detailed interactions between the 5′-end nucleotides (C15′–A13′) of tDNA and the MID binding pocket of SPARTA. The surface representation of CrtSPARTA reveals distinct spatial localization of the 15-bp gDNA–tDNA duplex ( G ) and 20-bp gRNA–tDNA duplex ( H ). ( I ) The superposition of the 15-bp gDNA–tDNA duplex with the 20-bp gRNA–tDNA duplex in CrtSPARTA complexes reveals distinct models for nucleic acid recognition.

    Techniques Used: Crystallization Assay, Binding Assay



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    The length of DNA target affects NADase activation. ( A ) SEC experiments assaying the binding ability of CrtSPARTA 1–421 to gDNA and tDNA of different lengths (5, 10, 15, and 21 nt). The peak fraction is analyzed by SDS–PAGE and TBE–urea PAGE. ( B ) The schematic representation of the gDNA and tDNA of different lengths. ( C ) NADase activity assays with 21-nt gDNA or gRNA and different lengths of tDNA. Data are shown as mean ± standard deviation ( n = 3 independent experiments).

    Journal: Nucleic Acids Research

    Article Title: Structural basis of ssDNA-guided NADase activation of prokaryotic SPARTA system

    doi: 10.1093/nar/gkaf110

    Figure Lengend Snippet: The length of DNA target affects NADase activation. ( A ) SEC experiments assaying the binding ability of CrtSPARTA 1–421 to gDNA and tDNA of different lengths (5, 10, 15, and 21 nt). The peak fraction is analyzed by SDS–PAGE and TBE–urea PAGE. ( B ) The schematic representation of the gDNA and tDNA of different lengths. ( C ) NADase activity assays with 21-nt gDNA or gRNA and different lengths of tDNA. Data are shown as mean ± standard deviation ( n = 3 independent experiments).

    Article Snippet: The gRNA and gDNA were chemically synthesized from GenScript.

    Techniques: Activation Assay, Binding Assay, SDS Page, Activity Assay, Standard Deviation

    Overall structure of CrtSPARTA 1–421 in complex with gDNA and 21-nt tDNA. ( A ) Schematic representation of 5′-P gDNA and tDNA oligonucleotides used for crystallization. ( B ) The overall structure of gDNA and 21-nt tDNA-bound CrtSPARTA 1–421 complex. ( C ) Schematic representation of the intermolecular contacts between SPARTA and guide–target duplex in the complex structure. The base, backbone sugar, and phosphate group of the gDNA and tDNA are shown as rectangles, pentagons, and circles, respectively. Protein residues are color-coded by their respective domains. ( D ) Electron density map of the gDNA–tDNA duplex. The 2mFo-Fc electron density map of the gDNA–tDNA duplex is shown as a mesh (contoured at 1.0σ). ( E ) Structure of the gDNA–tDNA duplex. ( F ) The gDNA–tDNA duplex binds in the positively charged channel of the CrtSPARTA. ( G ) Detailed interactions between the 3′-end nucleotides (A1′–T0′) of tDNA and the MID binding pocket of SPARTA. ( H ) Detailed interactions between the 5′-end nucleotides (T1–G2) of gDNA and the MID domain of SPARTA. The surface representation of CrtSPARTA reveals distinct spatial localization of the gDNA–tDNA duplex ( I ) and gRNA–tDNA duplex ( J ). ( K ) The superposition of the gDNA–tDNA duplex with the gRNA–tDNA duplex in CrtSPARTA complexes reveals distinct models for nucleic acid recognition.

    Journal: Nucleic Acids Research

    Article Title: Structural basis of ssDNA-guided NADase activation of prokaryotic SPARTA system

    doi: 10.1093/nar/gkaf110

    Figure Lengend Snippet: Overall structure of CrtSPARTA 1–421 in complex with gDNA and 21-nt tDNA. ( A ) Schematic representation of 5′-P gDNA and tDNA oligonucleotides used for crystallization. ( B ) The overall structure of gDNA and 21-nt tDNA-bound CrtSPARTA 1–421 complex. ( C ) Schematic representation of the intermolecular contacts between SPARTA and guide–target duplex in the complex structure. The base, backbone sugar, and phosphate group of the gDNA and tDNA are shown as rectangles, pentagons, and circles, respectively. Protein residues are color-coded by their respective domains. ( D ) Electron density map of the gDNA–tDNA duplex. The 2mFo-Fc electron density map of the gDNA–tDNA duplex is shown as a mesh (contoured at 1.0σ). ( E ) Structure of the gDNA–tDNA duplex. ( F ) The gDNA–tDNA duplex binds in the positively charged channel of the CrtSPARTA. ( G ) Detailed interactions between the 3′-end nucleotides (A1′–T0′) of tDNA and the MID binding pocket of SPARTA. ( H ) Detailed interactions between the 5′-end nucleotides (T1–G2) of gDNA and the MID domain of SPARTA. The surface representation of CrtSPARTA reveals distinct spatial localization of the gDNA–tDNA duplex ( I ) and gRNA–tDNA duplex ( J ). ( K ) The superposition of the gDNA–tDNA duplex with the gRNA–tDNA duplex in CrtSPARTA complexes reveals distinct models for nucleic acid recognition.

    Article Snippet: The gRNA and gDNA were chemically synthesized from GenScript.

    Techniques: Crystallization Assay, Binding Assay

    Overall architecture of CrtSPARTA 1–421 in complex with gDNA and 16-nt tDNA. ( A ) The sequences of 5′-P gDNA and 16-nt tDNA were used for crystallization. ( B ) The overall structure of gDNA and 16-nt tDNA-bound CrtSPARTA 1–421 complex. ( C ) Schematic representation of the intermolecular contacts between SPARTA and guide–target duplex in the complex structure. The base, backbone sugar, and phosphate group of the gDNA and tDNA are shown as rectangles, pentagons, and circles, respectively. Protein residues are color-coded by their respective domains. ( D ) Electron density map of the gDNA–tDNA duplex. The 2mFo-Fc electron density map of the gDNA–tDNA duplex is shown as a mesh (contoured at 1.0σ). ( E ) Detailed interactions between the nucleotides G15–A17 of gDNA and the MID and PIWI domains of SPARTA. ( F ) Detailed interactions between the 5′-end nucleotides (C15′–A13′) of tDNA and the MID binding pocket of SPARTA. The surface representation of CrtSPARTA reveals distinct spatial localization of the 15-bp gDNA–tDNA duplex ( G ) and 20-bp gRNA–tDNA duplex ( H ). ( I ) The superposition of the 15-bp gDNA–tDNA duplex with the 20-bp gRNA–tDNA duplex in CrtSPARTA complexes reveals distinct models for nucleic acid recognition.

    Journal: Nucleic Acids Research

    Article Title: Structural basis of ssDNA-guided NADase activation of prokaryotic SPARTA system

    doi: 10.1093/nar/gkaf110

    Figure Lengend Snippet: Overall architecture of CrtSPARTA 1–421 in complex with gDNA and 16-nt tDNA. ( A ) The sequences of 5′-P gDNA and 16-nt tDNA were used for crystallization. ( B ) The overall structure of gDNA and 16-nt tDNA-bound CrtSPARTA 1–421 complex. ( C ) Schematic representation of the intermolecular contacts between SPARTA and guide–target duplex in the complex structure. The base, backbone sugar, and phosphate group of the gDNA and tDNA are shown as rectangles, pentagons, and circles, respectively. Protein residues are color-coded by their respective domains. ( D ) Electron density map of the gDNA–tDNA duplex. The 2mFo-Fc electron density map of the gDNA–tDNA duplex is shown as a mesh (contoured at 1.0σ). ( E ) Detailed interactions between the nucleotides G15–A17 of gDNA and the MID and PIWI domains of SPARTA. ( F ) Detailed interactions between the 5′-end nucleotides (C15′–A13′) of tDNA and the MID binding pocket of SPARTA. The surface representation of CrtSPARTA reveals distinct spatial localization of the 15-bp gDNA–tDNA duplex ( G ) and 20-bp gRNA–tDNA duplex ( H ). ( I ) The superposition of the 15-bp gDNA–tDNA duplex with the 20-bp gRNA–tDNA duplex in CrtSPARTA complexes reveals distinct models for nucleic acid recognition.

    Article Snippet: The gRNA and gDNA were chemically synthesized from GenScript.

    Techniques: Crystallization Assay, Binding Assay