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q chen  (ATCC)


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    Structured Review

    ATCC q chen
    Q Chen, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 909 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/q+chen/pm41965753-289-16-9?v=ATCC
    Average 96 stars, based on 909 article reviews
    q chen - by Bioz Stars, 2026-07
    96/100 stars

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    Image Search Results


    ( a ) Representative cryo-EM micrograph; ( b ) Subset of representative, reference-free 2D class averages; ( c ) Data processing workflow.

    Journal: eLife

    Article Title: Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme

    doi: 10.7554/eLife.72535

    Figure Lengend Snippet: ( a ) Representative cryo-EM micrograph; ( b ) Subset of representative, reference-free 2D class averages; ( c ) Data processing workflow.

    Article Snippet: The following dataset was generated: Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2 RCSB Protein Data Bank 7V4H Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb decamer assembly RCSB Protein Data Bank 7V4I Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I RCSB Protein Data Bank 7V4J Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State II RCSB Protein Data Bank 7V4K Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State III RCSB Protein Data Bank 7V4L

    Techniques: Cryo-EM Sample Prep

    ( a ) Representative cryo-EM micrograph; ( b ) Subset of representative, reference-free 2D class averages; ( c ) Data processing workflow.

    Journal: eLife

    Article Title: Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme

    doi: 10.7554/eLife.72535

    Figure Lengend Snippet: ( a ) Representative cryo-EM micrograph; ( b ) Subset of representative, reference-free 2D class averages; ( c ) Data processing workflow.

    Article Snippet: The following dataset was generated: Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2 RCSB Protein Data Bank 7V4H Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb decamer assembly RCSB Protein Data Bank 7V4I Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I RCSB Protein Data Bank 7V4J Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State II RCSB Protein Data Bank 7V4K Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State III RCSB Protein Data Bank 7V4L

    Techniques: Cryo-EM Sample Prep

    ( a ) Structure alignment of three CsGSIb Pen structures determined using Cryo-EM. Left: Topview; Right: Sideview. These three structures, colored in golden, pink and purple, respectively, are highly similar to each other, with only a few structural variations at the peripheral regions. ( b–d ) Structure comparison of three structures of CsGSIb pentamer in isolation (colored the same as in a ) with that in the context of decamer (in color of green). Upper: Topview; Lower: Sideview. Note a large portion is missing in the structure of CsGSIb Pen arising from electron density missing, indicating those regions are highly dynamic.

    Journal: eLife

    Article Title: Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme

    doi: 10.7554/eLife.72535

    Figure Lengend Snippet: ( a ) Structure alignment of three CsGSIb Pen structures determined using Cryo-EM. Left: Topview; Right: Sideview. These three structures, colored in golden, pink and purple, respectively, are highly similar to each other, with only a few structural variations at the peripheral regions. ( b–d ) Structure comparison of three structures of CsGSIb pentamer in isolation (colored the same as in a ) with that in the context of decamer (in color of green). Upper: Topview; Lower: Sideview. Note a large portion is missing in the structure of CsGSIb Pen arising from electron density missing, indicating those regions are highly dynamic.

    Article Snippet: The following dataset was generated: Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2 RCSB Protein Data Bank 7V4H Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb decamer assembly RCSB Protein Data Bank 7V4I Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I RCSB Protein Data Bank 7V4J Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State II RCSB Protein Data Bank 7V4K Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State III RCSB Protein Data Bank 7V4L

    Techniques: Cryo-EM Sample Prep, Isolation

    For simplicity, only one out three CsGSIb Pen cryo-EM structures are presented here, and all three structures are shown in . ( a ) Local resolution of the density map of CsGSIb Pen indicates a decreased resolution near the edges of the pentamer ring. ( b ) Local resolution of the density map of CsGSIb Dec map. The conformational flexibility is apparent when the missing density at the rim of CsGSIb Pen , which yields a largely decagram-shaped map ( a ), is compared to the intact density of CsGSIb Dec that displays a pentagon-shaped map ( b ). ( c–d ) Superimposed of Cryo-EM structure of CsGSIb Pen (pink) with that of CsGSIb Dec (grey surface). ( c ): Top-view; ( d ): Side-view. The results reveal two major regions being highly disordered: the rim region including the catalytic center, and ring-ring interface. ( e ) Proposed activation mechanism model of CsGSIb.

    Journal: eLife

    Article Title: Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme

    doi: 10.7554/eLife.72535

    Figure Lengend Snippet: For simplicity, only one out three CsGSIb Pen cryo-EM structures are presented here, and all three structures are shown in . ( a ) Local resolution of the density map of CsGSIb Pen indicates a decreased resolution near the edges of the pentamer ring. ( b ) Local resolution of the density map of CsGSIb Dec map. The conformational flexibility is apparent when the missing density at the rim of CsGSIb Pen , which yields a largely decagram-shaped map ( a ), is compared to the intact density of CsGSIb Dec that displays a pentagon-shaped map ( b ). ( c–d ) Superimposed of Cryo-EM structure of CsGSIb Pen (pink) with that of CsGSIb Dec (grey surface). ( c ): Top-view; ( d ): Side-view. The results reveal two major regions being highly disordered: the rim region including the catalytic center, and ring-ring interface. ( e ) Proposed activation mechanism model of CsGSIb.

    Article Snippet: The following dataset was generated: Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2 RCSB Protein Data Bank 7V4H Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb decamer assembly RCSB Protein Data Bank 7V4I Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I RCSB Protein Data Bank 7V4J Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State II RCSB Protein Data Bank 7V4K Xu W Chen Y Xing Q Huang C 2021 Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State III RCSB Protein Data Bank 7V4L

    Techniques: Cryo-EM Sample Prep, Activation Assay