competent e coli 5α cells  (New England Biolabs)


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    New England Biolabs competent e coli 5α cells
    Competent E Coli 5α Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    t7 express de3 e coli competent cells  (New England Biolabs)


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    New England Biolabs t7 express de3 e coli competent cells
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    bl21 de3 e coli competent cells  (New England Biolabs)


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    New England Biolabs bl21 de3 e coli competent cells
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    5 alpha competent e coli cells  (New England Biolabs)


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    competent dh5 alpha e coli cells  (New England Biolabs)


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    New England Biolabs competent dh5 alpha e coli cells
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    5 alpha competent e coli cells  (New England Biolabs)


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    New England Biolabs 5 alpha competent e coli cells
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    e coli dh5α competent cells  (New England Biolabs)


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    New England Biolabs e coli dh5α competent cells

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    1) Product Images from "Flagellar-based motility accelerates IgA-mediated agglutination of Salmonella Typhimurium at high bacterial cell densities"

    Article Title: Flagellar-based motility accelerates IgA-mediated agglutination of Salmonella Typhimurium at high bacterial cell densities

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2023.1193855


    Figure Legend Snippet:

    Techniques Used:

    e coli bl21 de3 competent cells  (New England Biolabs)


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    New England Biolabs e coli bl21 de3 competent cells
    The COMMD proteins assemble into specific heteromeric complexes (A) Purification of COMMD sub-complexes. The ten human COMMD proteins were co-expressed in <t>E.</t> <t>coli</t> and purified via His-tags on different subunits followed by gel filtration. Peptide mass spectrometry identified the subunits co-purified with each tagged protein and reveals three distinct stable tetrameric complexes of COMMD1-6-4-8 (subcomplex A), COMMD2-3-4-8 (subcomplex B), and COMMD5-10-7-9 (subcomplex C). (B) 3.3-Å crystal structure of the tetrameric subcomplex C (COMMD5-10-7-9), primarily built around the three major binding interfaces shown in more detail below. (C) Key residues involved in the COMMD5-COMMD10 interface. (D) Key residues that form a β-sheet extension between COMMD5-COMMD10 and COMMD7-COMMD9 dimers. (E) Key COMMD10 residue Leu129 binds in a hydrophobic pocket to stabilize the tetramer. (F) The unique COMMD9 HN domain interface in which residues form stable and specific tetrameric interactions focusing on Trp157 of COMMD5. (G) Key interactions involving the COMMD9 linker between the HN and COMM domains centered around Ile118. (H) Similar to (F) showing the COMMD10 HN domain interactions with three subunits, centered on the COMMD7 Trp139 conserved sidechain.
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    1) Product Images from "Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome"

    Article Title: Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome

    Journal: Cell

    doi: 10.1016/j.cell.2023.04.003

    The COMMD proteins assemble into specific heteromeric complexes (A) Purification of COMMD sub-complexes. The ten human COMMD proteins were co-expressed in E. coli and purified via His-tags on different subunits followed by gel filtration. Peptide mass spectrometry identified the subunits co-purified with each tagged protein and reveals three distinct stable tetrameric complexes of COMMD1-6-4-8 (subcomplex A), COMMD2-3-4-8 (subcomplex B), and COMMD5-10-7-9 (subcomplex C). (B) 3.3-Å crystal structure of the tetrameric subcomplex C (COMMD5-10-7-9), primarily built around the three major binding interfaces shown in more detail below. (C) Key residues involved in the COMMD5-COMMD10 interface. (D) Key residues that form a β-sheet extension between COMMD5-COMMD10 and COMMD7-COMMD9 dimers. (E) Key COMMD10 residue Leu129 binds in a hydrophobic pocket to stabilize the tetramer. (F) The unique COMMD9 HN domain interface in which residues form stable and specific tetrameric interactions focusing on Trp157 of COMMD5. (G) Key interactions involving the COMMD9 linker between the HN and COMM domains centered around Ile118. (H) Similar to (F) showing the COMMD10 HN domain interactions with three subunits, centered on the COMMD7 Trp139 conserved sidechain.
    Figure Legend Snippet: The COMMD proteins assemble into specific heteromeric complexes (A) Purification of COMMD sub-complexes. The ten human COMMD proteins were co-expressed in E. coli and purified via His-tags on different subunits followed by gel filtration. Peptide mass spectrometry identified the subunits co-purified with each tagged protein and reveals three distinct stable tetrameric complexes of COMMD1-6-4-8 (subcomplex A), COMMD2-3-4-8 (subcomplex B), and COMMD5-10-7-9 (subcomplex C). (B) 3.3-Å crystal structure of the tetrameric subcomplex C (COMMD5-10-7-9), primarily built around the three major binding interfaces shown in more detail below. (C) Key residues involved in the COMMD5-COMMD10 interface. (D) Key residues that form a β-sheet extension between COMMD5-COMMD10 and COMMD7-COMMD9 dimers. (E) Key COMMD10 residue Leu129 binds in a hydrophobic pocket to stabilize the tetramer. (F) The unique COMMD9 HN domain interface in which residues form stable and specific tetrameric interactions focusing on Trp157 of COMMD5. (G) Key interactions involving the COMMD9 linker between the HN and COMM domains centered around Ile118. (H) Similar to (F) showing the COMMD10 HN domain interactions with three subunits, centered on the COMMD7 Trp139 conserved sidechain.

    Techniques Used: Purification, Filtration, Mass Spectrometry, Binding Assay


    Figure Legend Snippet:

    Techniques Used: Strep-tag, FLAG-tag, Knock-Out, Transfection, Recombinant, Plasmid Preparation, Electron Microscopy, Sequencing, Software

    competent e coli cells  (New England Biolabs)


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    New England Biolabs competent e coli cells
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    New England Biolabs e coli bl21 de3 competent cells
    The COMMD proteins assemble into specific heteromeric complexes (A) Purification of COMMD sub-complexes. The ten human COMMD proteins were co-expressed in <t>E.</t> <t>coli</t> and purified via His-tags on different subunits followed by gel filtration. Peptide mass spectrometry identified the subunits co-purified with each tagged protein and reveals three distinct stable tetrameric complexes of COMMD1-6-4-8 (subcomplex A), COMMD2-3-4-8 (subcomplex B), and COMMD5-10-7-9 (subcomplex C). (B) 3.3-Å crystal structure of the tetrameric subcomplex C (COMMD5-10-7-9), primarily built around the three major binding interfaces shown in more detail below. (C) Key residues involved in the COMMD5-COMMD10 interface. (D) Key residues that form a β-sheet extension between COMMD5-COMMD10 and COMMD7-COMMD9 dimers. (E) Key COMMD10 residue Leu129 binds in a hydrophobic pocket to stabilize the tetramer. (F) The unique COMMD9 HN domain interface in which residues form stable and specific tetrameric interactions focusing on Trp157 of COMMD5. (G) Key interactions involving the COMMD9 linker between the HN and COMM domains centered around Ile118. (H) Similar to (F) showing the COMMD10 HN domain interactions with three subunits, centered on the COMMD7 Trp139 conserved sidechain.
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    The COMMD proteins assemble into specific heteromeric complexes (A) Purification of COMMD sub-complexes. The ten human COMMD proteins were co-expressed in <t>E.</t> <t>coli</t> and purified via His-tags on different subunits followed by gel filtration. Peptide mass spectrometry identified the subunits co-purified with each tagged protein and reveals three distinct stable tetrameric complexes of COMMD1-6-4-8 (subcomplex A), COMMD2-3-4-8 (subcomplex B), and COMMD5-10-7-9 (subcomplex C). (B) 3.3-Å crystal structure of the tetrameric subcomplex C (COMMD5-10-7-9), primarily built around the three major binding interfaces shown in more detail below. (C) Key residues involved in the COMMD5-COMMD10 interface. (D) Key residues that form a β-sheet extension between COMMD5-COMMD10 and COMMD7-COMMD9 dimers. (E) Key COMMD10 residue Leu129 binds in a hydrophobic pocket to stabilize the tetramer. (F) The unique COMMD9 HN domain interface in which residues form stable and specific tetrameric interactions focusing on Trp157 of COMMD5. (G) Key interactions involving the COMMD9 linker between the HN and COMM domains centered around Ile118. (H) Similar to (F) showing the COMMD10 HN domain interactions with three subunits, centered on the COMMD7 Trp139 conserved sidechain.
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    The COMMD proteins assemble into specific heteromeric complexes (A) Purification of COMMD sub-complexes. The ten human COMMD proteins were co-expressed in <t>E.</t> <t>coli</t> and purified via His-tags on different subunits followed by gel filtration. Peptide mass spectrometry identified the subunits co-purified with each tagged protein and reveals three distinct stable tetrameric complexes of COMMD1-6-4-8 (subcomplex A), COMMD2-3-4-8 (subcomplex B), and COMMD5-10-7-9 (subcomplex C). (B) 3.3-Å crystal structure of the tetrameric subcomplex C (COMMD5-10-7-9), primarily built around the three major binding interfaces shown in more detail below. (C) Key residues involved in the COMMD5-COMMD10 interface. (D) Key residues that form a β-sheet extension between COMMD5-COMMD10 and COMMD7-COMMD9 dimers. (E) Key COMMD10 residue Leu129 binds in a hydrophobic pocket to stabilize the tetramer. (F) The unique COMMD9 HN domain interface in which residues form stable and specific tetrameric interactions focusing on Trp157 of COMMD5. (G) Key interactions involving the COMMD9 linker between the HN and COMM domains centered around Ile118. (H) Similar to (F) showing the COMMD10 HN domain interactions with three subunits, centered on the COMMD7 Trp139 conserved sidechain.
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    Journal: Frontiers in Immunology

    Article Title: Flagellar-based motility accelerates IgA-mediated agglutination of Salmonella Typhimurium at high bacterial cell densities

    doi: 10.3389/fimmu.2023.1193855

    Figure Lengend Snippet:

    Article Snippet: E. coli DH5α competent cells were transformed with the resulting yhjH construct (NEB).

    Techniques:

    The COMMD proteins assemble into specific heteromeric complexes (A) Purification of COMMD sub-complexes. The ten human COMMD proteins were co-expressed in E. coli and purified via His-tags on different subunits followed by gel filtration. Peptide mass spectrometry identified the subunits co-purified with each tagged protein and reveals three distinct stable tetrameric complexes of COMMD1-6-4-8 (subcomplex A), COMMD2-3-4-8 (subcomplex B), and COMMD5-10-7-9 (subcomplex C). (B) 3.3-Å crystal structure of the tetrameric subcomplex C (COMMD5-10-7-9), primarily built around the three major binding interfaces shown in more detail below. (C) Key residues involved in the COMMD5-COMMD10 interface. (D) Key residues that form a β-sheet extension between COMMD5-COMMD10 and COMMD7-COMMD9 dimers. (E) Key COMMD10 residue Leu129 binds in a hydrophobic pocket to stabilize the tetramer. (F) The unique COMMD9 HN domain interface in which residues form stable and specific tetrameric interactions focusing on Trp157 of COMMD5. (G) Key interactions involving the COMMD9 linker between the HN and COMM domains centered around Ile118. (H) Similar to (F) showing the COMMD10 HN domain interactions with three subunits, centered on the COMMD7 Trp139 conserved sidechain.

    Journal: Cell

    Article Title: Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome

    doi: 10.1016/j.cell.2023.04.003

    Figure Lengend Snippet: The COMMD proteins assemble into specific heteromeric complexes (A) Purification of COMMD sub-complexes. The ten human COMMD proteins were co-expressed in E. coli and purified via His-tags on different subunits followed by gel filtration. Peptide mass spectrometry identified the subunits co-purified with each tagged protein and reveals three distinct stable tetrameric complexes of COMMD1-6-4-8 (subcomplex A), COMMD2-3-4-8 (subcomplex B), and COMMD5-10-7-9 (subcomplex C). (B) 3.3-Å crystal structure of the tetrameric subcomplex C (COMMD5-10-7-9), primarily built around the three major binding interfaces shown in more detail below. (C) Key residues involved in the COMMD5-COMMD10 interface. (D) Key residues that form a β-sheet extension between COMMD5-COMMD10 and COMMD7-COMMD9 dimers. (E) Key COMMD10 residue Leu129 binds in a hydrophobic pocket to stabilize the tetramer. (F) The unique COMMD9 HN domain interface in which residues form stable and specific tetrameric interactions focusing on Trp157 of COMMD5. (G) Key interactions involving the COMMD9 linker between the HN and COMM domains centered around Ile118. (H) Similar to (F) showing the COMMD10 HN domain interactions with three subunits, centered on the COMMD7 Trp139 conserved sidechain.

    Article Snippet: The bacterial expression plasmids were transformed into E. coli BL21 DE3 competent cells (New England Biolabs) and plated on agar plates containing ampicillin.

    Techniques: Purification, Filtration, Mass Spectrometry, Binding Assay

    Journal: Cell

    Article Title: Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome

    doi: 10.1016/j.cell.2023.04.003

    Figure Lengend Snippet:

    Article Snippet: The bacterial expression plasmids were transformed into E. coli BL21 DE3 competent cells (New England Biolabs) and plated on agar plates containing ampicillin.

    Techniques: Strep-tag, FLAG-tag, Knock-Out, Transfection, Recombinant, Plasmid Preparation, Electron Microscopy, Sequencing, Software