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  • 99
    ATCC subclone 14
    Subclone 14, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore subcloning bovine as
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    Promega subcloning
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    Thermo Fisher subcloning
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    TaKaRa subcloning timer
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    Promega ta subcloning
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    Oxford Expression Technologies Ltd sf9 subclone
    SDS-PAGE and Western blot analysis of final purified Pfs230C1. (A) SDS-PAGE under non-reducing and reducing conditions followed by silver stain. (B) Western blot with anti-his antibody. (A–B) Lanes 1–2 representative Pfs230C1 from the original Super <t>Sf9</t> process [ 16 ], and Lanes 3–4 Pfs230C1 derived from 20 L optimized process. Non-reducing (Lanes 1, 4) and reducing (Lanes 2, 3) conditions. Western blot analysis of (C) Pfs230C1 and (D) native parasite extracts with mouse monoclonal antibody 15A4-1B12 under reducing (R) and non-reducing (NR) conditions. Different molecular weight marker standards are utilized for panels C and D given the difference in molecular weight of target protein. Expected molecular weight of native Pfs230 is ∼363 kDa, however, since protease inhibitors are not utilized, multiple bands are visible.
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    82
    Promega subcloning notebook
    SDS-PAGE and Western blot analysis of final purified Pfs230C1. (A) SDS-PAGE under non-reducing and reducing conditions followed by silver stain. (B) Western blot with anti-his antibody. (A–B) Lanes 1–2 representative Pfs230C1 from the original Super <t>Sf9</t> process [ 16 ], and Lanes 3–4 Pfs230C1 derived from 20 L optimized process. Non-reducing (Lanes 1, 4) and reducing (Lanes 2, 3) conditions. Western blot analysis of (C) Pfs230C1 and (D) native parasite extracts with mouse monoclonal antibody 15A4-1B12 under reducing (R) and non-reducing (NR) conditions. Different molecular weight marker standards are utilized for panels C and D given the difference in molecular weight of target protein. Expected molecular weight of native Pfs230 is ∼363 kDa, however, since protease inhibitors are not utilized, multiple bands are visible.
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    99
    ATCC subclone 4
    SDS-PAGE and Western blot analysis of final purified Pfs230C1. (A) SDS-PAGE under non-reducing and reducing conditions followed by silver stain. (B) Western blot with anti-his antibody. (A–B) Lanes 1–2 representative Pfs230C1 from the original Super <t>Sf9</t> process [ 16 ], and Lanes 3–4 Pfs230C1 derived from 20 L optimized process. Non-reducing (Lanes 1, 4) and reducing (Lanes 2, 3) conditions. Western blot analysis of (C) Pfs230C1 and (D) native parasite extracts with mouse monoclonal antibody 15A4-1B12 under reducing (R) and non-reducing (NR) conditions. Different molecular weight marker standards are utilized for panels C and D given the difference in molecular weight of target protein. Expected molecular weight of native Pfs230 is ∼363 kDa, however, since protease inhibitors are not utilized, multiple bands are visible.
    Subclone 4, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher subcloning efficiency
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    99
    ATCC subclone 24
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
    Subclone 24, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher subcloning eyfp
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Thermo Fisher ligase free subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    87
    Thermo Fisher subcloning puno1 hcd200
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    93
    Thermo Fisher gateway subcloning system
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    94
    Addgene inc subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Agilent technologies subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Genewiz subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    GenScript subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    OriGene subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Stratagene subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Syntaxin subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Millipore subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Thermo Fisher topo subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Gene Bridges Inc subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    ViraQuest Inc subcloning
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    ATCC mc3t3 e1 subclone c14
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Gene Bridges Inc bac subcloning kit
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    79
    Addgene inc pcr subcloning akt2
    D1 anaerobic protein purity. Protein was expressed in <t>DH5α</t> from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).
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    Image Search Results


    SDS-PAGE and Western blot analysis of final purified Pfs230C1. (A) SDS-PAGE under non-reducing and reducing conditions followed by silver stain. (B) Western blot with anti-his antibody. (A–B) Lanes 1–2 representative Pfs230C1 from the original Super Sf9 process [ 16 ], and Lanes 3–4 Pfs230C1 derived from 20 L optimized process. Non-reducing (Lanes 1, 4) and reducing (Lanes 2, 3) conditions. Western blot analysis of (C) Pfs230C1 and (D) native parasite extracts with mouse monoclonal antibody 15A4-1B12 under reducing (R) and non-reducing (NR) conditions. Different molecular weight marker standards are utilized for panels C and D given the difference in molecular weight of target protein. Expected molecular weight of native Pfs230 is ∼363 kDa, however, since protease inhibitors are not utilized, multiple bands are visible.

    Journal: Protein Expression and Purification

    Article Title: Expression and purification optimization of an N-terminal Pfs230 transmission-blocking vaccine candidate

    doi: 10.1016/j.pep.2019.04.001

    Figure Lengend Snippet: SDS-PAGE and Western blot analysis of final purified Pfs230C1. (A) SDS-PAGE under non-reducing and reducing conditions followed by silver stain. (B) Western blot with anti-his antibody. (A–B) Lanes 1–2 representative Pfs230C1 from the original Super Sf9 process [ 16 ], and Lanes 3–4 Pfs230C1 derived from 20 L optimized process. Non-reducing (Lanes 1, 4) and reducing (Lanes 2, 3) conditions. Western blot analysis of (C) Pfs230C1 and (D) native parasite extracts with mouse monoclonal antibody 15A4-1B12 under reducing (R) and non-reducing (NR) conditions. Different molecular weight marker standards are utilized for panels C and D given the difference in molecular weight of target protein. Expected molecular weight of native Pfs230 is ∼363 kDa, however, since protease inhibitors are not utilized, multiple bands are visible.

    Article Snippet: Super Sf9 is a genetically engineered Sf9 subclone (Oxford Expression Technologies).

    Techniques: SDS Page, Western Blot, Purification, Silver Staining, Derivative Assay, Molecular Weight, Marker

    SDS-PAGE Freeze/thaw stability analysis of final purified Pfs230C1 under non-reducing (A) and reducing (B) conditions followed by silver stain. Reference Pfs230C1 from previous [ 16 ] Super Sf9 process (Lanes 1–2). Pfs230C1 from 20 L optimized process after one (Lanes 3–4) three (Lanes 5–6) and five (lanes 7–8) freeze/thaw cycles. Proteins loaded at 1 μg (Lanes 1, 3, 5, 7) and 5 μg (Lanes 2, 4, 6, 8).

    Journal: Protein Expression and Purification

    Article Title: Expression and purification optimization of an N-terminal Pfs230 transmission-blocking vaccine candidate

    doi: 10.1016/j.pep.2019.04.001

    Figure Lengend Snippet: SDS-PAGE Freeze/thaw stability analysis of final purified Pfs230C1 under non-reducing (A) and reducing (B) conditions followed by silver stain. Reference Pfs230C1 from previous [ 16 ] Super Sf9 process (Lanes 1–2). Pfs230C1 from 20 L optimized process after one (Lanes 3–4) three (Lanes 5–6) and five (lanes 7–8) freeze/thaw cycles. Proteins loaded at 1 μg (Lanes 1, 3, 5, 7) and 5 μg (Lanes 2, 4, 6, 8).

    Article Snippet: Super Sf9 is a genetically engineered Sf9 subclone (Oxford Expression Technologies).

    Techniques: SDS Page, Purification, Silver Staining

    (A) SDS-PAGE and (B) Western blot (anti-his antibody) analysis of purified Pfs230C1 from Super Sf9 (Lanes 1–2), Sf9 (Lanes 3–4) and High Five cells (Lanes 5–6). Samples loaded under non-reducing (Lanes 1, 3, 5) and reducing (Lanes 2, 4, 6) conditions. Arrows indicate the target Pfs230C1 protein.

    Journal: Protein Expression and Purification

    Article Title: Expression and purification optimization of an N-terminal Pfs230 transmission-blocking vaccine candidate

    doi: 10.1016/j.pep.2019.04.001

    Figure Lengend Snippet: (A) SDS-PAGE and (B) Western blot (anti-his antibody) analysis of purified Pfs230C1 from Super Sf9 (Lanes 1–2), Sf9 (Lanes 3–4) and High Five cells (Lanes 5–6). Samples loaded under non-reducing (Lanes 1, 3, 5) and reducing (Lanes 2, 4, 6) conditions. Arrows indicate the target Pfs230C1 protein.

    Article Snippet: Super Sf9 is a genetically engineered Sf9 subclone (Oxford Expression Technologies).

    Techniques: SDS Page, Western Blot, Purification

    D1 anaerobic protein purity. Protein was expressed in DH5α from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).

    Journal: Protein expression and purification

    Article Title: Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization

    doi: 10.1016/j.pep.2017.03.019

    Figure Lengend Snippet: D1 anaerobic protein purity. Protein was expressed in DH5α from the pASG-IBA35 vector A. Steps of D1 anaerobic purification process. Numbers above the gel mark fractions: 1 – before induction, 2- after induction, 3 – lysate, 4- pellet after centrifugation at 40 000 rcf, 5- NiNTA flow through, 6 – elution (this D1 anaerobic protein batch was used for EXAFS experiments). The marked band with mass 30 kDa corresponds to D1 protein. B. The purity of D1 anaerobic protein batch used for TSA, crystallization and SEC HPLC analysis (lanes 1 and 2).

    Article Snippet: During the course of the study two E. coli strains, DH5α (#18265017, LifeTechnologies) and BL21(DE3)RILP (#230280, Agilent Technologies) were used.

    Techniques: Plasmid Preparation, Purification, Centrifugation, Flow Cytometry, Crystallization Assay, Size-exclusion Chromatography, High Performance Liquid Chromatography