e. coli bluescript vector (pbs Search Results


t7 express lysy competent cells  (New England Biolabs)
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New England Biolabs t7 express lysy competent cells
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e coli 269 bl21 de3  (GE Healthcare)
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GE Healthcare e coli 269 bl21 de3
E Coli 269 Bl21 De3, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e. coli strain xl-l blue chemically competent cells  (Agilent technologies)
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Agilent technologies e. coli strain xl-l blue chemically competent cells
E. Coli Strain Xl L Blue Chemically Competent Cells, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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manuscript n a albuminz bovine albumin low igg  (Valiant Co Ltd)
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Valiant Co Ltd manuscript n a albuminz bovine albumin low igg
Manuscript N A Albuminz Bovine Albumin Low Igg, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e coli destination vector pdest 566  (Addgene inc)
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Addgene inc e coli destination vector pdest 566
E Coli Destination Vector Pdest 566, supplied by Addgene inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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escherichia coli strain bl21(de3  (Millipore)
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Millipore escherichia coli strain bl21(de3
Escherichia Coli Strain Bl21(De3, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e. coli bl21-codonplus (de3)-ril-x strain  (Agilent technologies)
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Agilent technologies e. coli bl21-codonplus (de3)-ril-x strain
E. Coli Bl21 Codonplus (De3) Ril X Strain, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e. coli bl21 (de3) cells  (Addgene inc)
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Addgene inc e. coli bl21 (de3) cells
Cas1–2/3 complex does not obscure binding sites for DNA or anti-CRISPR AcrF3. (A) The DNA binding surface on Cas1–Cas2 is not blocked within the Cas1–2/3 complex. (B) DNA binding by the <t>E.</t> <t>coli</t> I-E Cas1–Cas2 complex induces a conformational change in the Cas1 dimers. Docking the crystal structure of this DNA-bound complex (PDB ID code 5DS5) into the Cas1–2/3 EM density reveals a steric clash between Cas1 and Cas2/3. (C) A 90-degree rotation of the Cas1–2/3 complex showing ssDNA modeled into the binding cleft (green) of the Cas3 domain. The DNA was positioned in this model by superimposing the crystal structure of I-E Cas3 from Thermobifida fusca bound to ssDNA (PDB ID code 4QQW) onto the Cas3 domain of the Cas2/3 protein from P. aeruginosa (PDB ID code 5B7I). (D) The structure of Cas2/3 with anti-CRISPR AcrF3 (PDB ID code 5B7I) bound reveals the HD nuclease active site is not obscured. (E) The positions of anti-CRISPR–bound Cas2/3 and Cas1 within the pseudoatomic model indicate separate binding sites for Cas1 and AcrF3.
E. Coli Bl21 (De3) Cells, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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petri dishes  (Corning Life Sciences)
90
Corning Life Sciences petri dishes
Cas1–2/3 complex does not obscure binding sites for DNA or anti-CRISPR AcrF3. (A) The DNA binding surface on Cas1–Cas2 is not blocked within the Cas1–2/3 complex. (B) DNA binding by the <t>E.</t> <t>coli</t> I-E Cas1–Cas2 complex induces a conformational change in the Cas1 dimers. Docking the crystal structure of this DNA-bound complex (PDB ID code 5DS5) into the Cas1–2/3 EM density reveals a steric clash between Cas1 and Cas2/3. (C) A 90-degree rotation of the Cas1–2/3 complex showing ssDNA modeled into the binding cleft (green) of the Cas3 domain. The DNA was positioned in this model by superimposing the crystal structure of I-E Cas3 from Thermobifida fusca bound to ssDNA (PDB ID code 4QQW) onto the Cas3 domain of the Cas2/3 protein from P. aeruginosa (PDB ID code 5B7I). (D) The structure of Cas2/3 with anti-CRISPR AcrF3 (PDB ID code 5B7I) bound reveals the HD nuclease active site is not obscured. (E) The positions of anti-CRISPR–bound Cas2/3 and Cas1 within the pseudoatomic model indicate separate binding sites for Cas1 and AcrF3.
Petri Dishes, supplied by Corning Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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bl21 de3 strain  (New England Biolabs)
99
New England Biolabs bl21 de3 strain
Cas1–2/3 complex does not obscure binding sites for DNA or anti-CRISPR AcrF3. (A) The DNA binding surface on Cas1–Cas2 is not blocked within the Cas1–2/3 complex. (B) DNA binding by the <t>E.</t> <t>coli</t> I-E Cas1–Cas2 complex induces a conformational change in the Cas1 dimers. Docking the crystal structure of this DNA-bound complex (PDB ID code 5DS5) into the Cas1–2/3 EM density reveals a steric clash between Cas1 and Cas2/3. (C) A 90-degree rotation of the Cas1–2/3 complex showing ssDNA modeled into the binding cleft (green) of the Cas3 domain. The DNA was positioned in this model by superimposing the crystal structure of I-E Cas3 from Thermobifida fusca bound to ssDNA (PDB ID code 4QQW) onto the Cas3 domain of the Cas2/3 protein from P. aeruginosa (PDB ID code 5B7I). (D) The structure of Cas2/3 with anti-CRISPR AcrF3 (PDB ID code 5B7I) bound reveals the HD nuclease active site is not obscured. (E) The positions of anti-CRISPR–bound Cas2/3 and Cas1 within the pseudoatomic model indicate separate binding sites for Cas1 and AcrF3.
Bl21 De3 Strain, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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escherichia coli expression vector pmal c2x  (New England Biolabs)
86
New England Biolabs escherichia coli expression vector pmal c2x
Cas1–2/3 complex does not obscure binding sites for DNA or anti-CRISPR AcrF3. (A) The DNA binding surface on Cas1–Cas2 is not blocked within the Cas1–2/3 complex. (B) DNA binding by the <t>E.</t> <t>coli</t> I-E Cas1–Cas2 complex induces a conformational change in the Cas1 dimers. Docking the crystal structure of this DNA-bound complex (PDB ID code 5DS5) into the Cas1–2/3 EM density reveals a steric clash between Cas1 and Cas2/3. (C) A 90-degree rotation of the Cas1–2/3 complex showing ssDNA modeled into the binding cleft (green) of the Cas3 domain. The DNA was positioned in this model by superimposing the crystal structure of I-E Cas3 from Thermobifida fusca bound to ssDNA (PDB ID code 4QQW) onto the Cas3 domain of the Cas2/3 protein from P. aeruginosa (PDB ID code 5B7I). (D) The structure of Cas2/3 with anti-CRISPR AcrF3 (PDB ID code 5B7I) bound reveals the HD nuclease active site is not obscured. (E) The positions of anti-CRISPR–bound Cas2/3 and Cas1 within the pseudoatomic model indicate separate binding sites for Cas1 and AcrF3.
Escherichia Coli Expression Vector Pmal C2x, 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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rosetta2 (de3) plyss e. coli cells  (Merck KGaA)
90
Merck KGaA rosetta2 (de3) plyss e. coli cells
Cas1–2/3 complex does not obscure binding sites for DNA or anti-CRISPR AcrF3. (A) The DNA binding surface on Cas1–Cas2 is not blocked within the Cas1–2/3 complex. (B) DNA binding by the <t>E.</t> <t>coli</t> I-E Cas1–Cas2 complex induces a conformational change in the Cas1 dimers. Docking the crystal structure of this DNA-bound complex (PDB ID code 5DS5) into the Cas1–2/3 EM density reveals a steric clash between Cas1 and Cas2/3. (C) A 90-degree rotation of the Cas1–2/3 complex showing ssDNA modeled into the binding cleft (green) of the Cas3 domain. The DNA was positioned in this model by superimposing the crystal structure of I-E Cas3 from Thermobifida fusca bound to ssDNA (PDB ID code 4QQW) onto the Cas3 domain of the Cas2/3 protein from P. aeruginosa (PDB ID code 5B7I). (D) The structure of Cas2/3 with anti-CRISPR AcrF3 (PDB ID code 5B7I) bound reveals the HD nuclease active site is not obscured. (E) The positions of anti-CRISPR–bound Cas2/3 and Cas1 within the pseudoatomic model indicate separate binding sites for Cas1 and AcrF3.
Rosetta2 (De3) Plyss E. Coli Cells, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Cas1–2/3 complex does not obscure binding sites for DNA or anti-CRISPR AcrF3. (A) The DNA binding surface on Cas1–Cas2 is not blocked within the Cas1–2/3 complex. (B) DNA binding by the E. coli I-E Cas1–Cas2 complex induces a conformational change in the Cas1 dimers. Docking the crystal structure of this DNA-bound complex (PDB ID code 5DS5) into the Cas1–2/3 EM density reveals a steric clash between Cas1 and Cas2/3. (C) A 90-degree rotation of the Cas1–2/3 complex showing ssDNA modeled into the binding cleft (green) of the Cas3 domain. The DNA was positioned in this model by superimposing the crystal structure of I-E Cas3 from Thermobifida fusca bound to ssDNA (PDB ID code 4QQW) onto the Cas3 domain of the Cas2/3 protein from P. aeruginosa (PDB ID code 5B7I). (D) The structure of Cas2/3 with anti-CRISPR AcrF3 (PDB ID code 5B7I) bound reveals the HD nuclease active site is not obscured. (E) The positions of anti-CRISPR–bound Cas2/3 and Cas1 within the pseudoatomic model indicate separate binding sites for Cas1 and AcrF3.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: Cas1 and the Csy complex are opposing regulators of Cas2/3 nuclease activity

doi: 10.1073/pnas.1616395114

Figure Lengend Snippet: Cas1–2/3 complex does not obscure binding sites for DNA or anti-CRISPR AcrF3. (A) The DNA binding surface on Cas1–Cas2 is not blocked within the Cas1–2/3 complex. (B) DNA binding by the E. coli I-E Cas1–Cas2 complex induces a conformational change in the Cas1 dimers. Docking the crystal structure of this DNA-bound complex (PDB ID code 5DS5) into the Cas1–2/3 EM density reveals a steric clash between Cas1 and Cas2/3. (C) A 90-degree rotation of the Cas1–2/3 complex showing ssDNA modeled into the binding cleft (green) of the Cas3 domain. The DNA was positioned in this model by superimposing the crystal structure of I-E Cas3 from Thermobifida fusca bound to ssDNA (PDB ID code 4QQW) onto the Cas3 domain of the Cas2/3 protein from P. aeruginosa (PDB ID code 5B7I). (D) The structure of Cas2/3 with anti-CRISPR AcrF3 (PDB ID code 5B7I) bound reveals the HD nuclease active site is not obscured. (E) The positions of anti-CRISPR–bound Cas2/3 and Cas1 within the pseudoatomic model indicate separate binding sites for Cas1 and AcrF3.

Article Snippet: Csy genes and a synthetic CRISPR were coexpressed on separate vectors in E. coli BL21 (DE3) cells as previously described ( 32 , 59 ) (AddGene ID 89232, 89244).

Techniques: Binding Assay, CRISPR