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Bruker Corporation elexsys 580 spectrometer
Elexsys 580 Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 99/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/elexsys 580 spectrometer/product/Bruker Corporation
Average 99 stars, based on 40 article reviews
Price from $9.99 to $1999.99
elexsys 580 spectrometer - by Bioz Stars, 2022-10
99/100 stars

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    Bruker Corporation q band bruker elexsys 580 spectrometer
    SrtA is a dynamic protein that undergoes a large conformational change upon substrate binding. A) Residues selected for mutagenesis for spin-label incorporation are labeled and their positions are shown in the NMR (top) or x-ray crystal structure (bottom) models. B) Distance distribution plots of SrtA variants with pairs of spin labels incorporated at the indicated positions in the absence (solid line) or presence of sort-tag substrate peptide (dashed line). The colored distributions represent the predicted distances obtained from PRONOX using the x-ray (blue; PDB: 1T2W) and NMR models (gray; PDB: 2KID-1). The background-corrected dipolar evolution data (gray dots) are shown for each pair of spin labeled mutant SrtA proteins (100 μM) as recorded on a Q-band <t>Bruker</t> <t>ELEXSYS</t> 580 spectrometer (Fig B in S1 File for the raw data); the black lines represent the fits to the data in the absence of substrate and the blue lines represent the fits to the data for the SrtA protein in the presence of 10x Abz-CLEPTGG.
    Q Band Bruker Elexsys 580 Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 99/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/q band bruker elexsys 580 spectrometer/product/Bruker Corporation
    Average 99 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    q band bruker elexsys 580 spectrometer - by Bioz Stars, 2022-10
    99/100 stars
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    SrtA is a dynamic protein that undergoes a large conformational change upon substrate binding. A) Residues selected for mutagenesis for spin-label incorporation are labeled and their positions are shown in the NMR (top) or x-ray crystal structure (bottom) models. B) Distance distribution plots of SrtA variants with pairs of spin labels incorporated at the indicated positions in the absence (solid line) or presence of sort-tag substrate peptide (dashed line). The colored distributions represent the predicted distances obtained from PRONOX using the x-ray (blue; PDB: 1T2W) and NMR models (gray; PDB: 2KID-1). The background-corrected dipolar evolution data (gray dots) are shown for each pair of spin labeled mutant SrtA proteins (100 μM) as recorded on a Q-band Bruker ELEXSYS 580 spectrometer (Fig B in S1 File for the raw data); the black lines represent the fits to the data in the absence of substrate and the blue lines represent the fits to the data for the SrtA protein in the presence of 10x Abz-CLEPTGG.

    Journal: PLoS ONE

    Article Title: Directed evolution provides insight into conformational substrate sampling by SrtA

    doi: 10.1371/journal.pone.0184271

    Figure Lengend Snippet: SrtA is a dynamic protein that undergoes a large conformational change upon substrate binding. A) Residues selected for mutagenesis for spin-label incorporation are labeled and their positions are shown in the NMR (top) or x-ray crystal structure (bottom) models. B) Distance distribution plots of SrtA variants with pairs of spin labels incorporated at the indicated positions in the absence (solid line) or presence of sort-tag substrate peptide (dashed line). The colored distributions represent the predicted distances obtained from PRONOX using the x-ray (blue; PDB: 1T2W) and NMR models (gray; PDB: 2KID-1). The background-corrected dipolar evolution data (gray dots) are shown for each pair of spin labeled mutant SrtA proteins (100 μM) as recorded on a Q-band Bruker ELEXSYS 580 spectrometer (Fig B in S1 File for the raw data); the black lines represent the fits to the data in the absence of substrate and the blue lines represent the fits to the data for the SrtA protein in the presence of 10x Abz-CLEPTGG.

    Article Snippet: Fig B in S1 File: The raw dipolar evolution data (gray dots) and backgrounds (solid lines) are shown for each pair of spin labeled mutant SrtA proteins (100 μM) as recorded on a Q-band Bruker ELEXSYS 580 spectrometer.

    Techniques: Binding Assay, Mutagenesis, Labeling, Nuclear Magnetic Resonance