buffer 500 mm nacl Search Results


500 mm nacl buffer (4 ml/g of tissue weight)  (Fisher Scientific)
90
Fisher Scientific 500 mm nacl buffer (4 ml/g of tissue weight)
500 Mm Nacl Buffer (4 Ml/G Of Tissue Weight), supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/500 mm nacl buffer (4 ml/g of tissue weight)/product/Fisher Scientific
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500 mm nacl buffer (4 ml/g of tissue weight) - by Bioz Stars, 2026-03
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mda-05-2782 (n e = 1.6152, n o = 1.4912, measured at 589.3 nm and 20 °c, clearing point: 106 °c)  (Merck KGaA)
90
Merck KGaA mda-05-2782 (n e = 1.6152, n o = 1.4912, measured at 589.3 nm and 20 °c, clearing point: 106 °c)
Mda 05 2782 (N E = 1.6152, N O = 1.4912, Measured At 589.3 Nm And 20 °C, Clearing Point: 106 °C), 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
https://www.bioz.com/result/mda-05-2782 (n e = 1.6152, n o = 1.4912, measured at 589.3 nm and 20 °c, clearing point: 106 °c)/product/Merck KGaA
Average 90 stars, based on 1 article reviews
mda-05-2782 (n e = 1.6152, n o = 1.4912, measured at 589.3 nm and 20 °c, clearing point: 106 °c) - by Bioz Stars, 2026-03
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11 μl of 10× proteinase k buffer (100 mm tris-hcl [ph 8.0], 500 mm nacl, 50 mm edta)  (IBI Scientific)
90
IBI Scientific 11 μl of 10× proteinase k buffer (100 mm tris-hcl [ph 8.0], 500 mm nacl, 50 mm edta)
11 μl Of 10× Proteinase K Buffer (100 Mm Tris Hcl [Ph 8.0], 500 Mm Nacl, 50 Mm Edta), supplied by IBI Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/11 μl of 10× proteinase k buffer (100 mm tris-hcl [ph 8.0], 500 mm nacl, 50 mm edta)/product/IBI Scientific
Average 90 stars, based on 1 article reviews
11 μl of 10× proteinase k buffer (100 mm tris-hcl [ph 8.0], 500 mm nacl, 50 mm edta) - by Bioz Stars, 2026-03
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phosphate buffered saline (pbs)  (Seikagaku corporation)
90
Seikagaku corporation phosphate buffered saline (pbs)
Phosphate Buffered Saline (Pbs), supplied by Seikagaku corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/phosphate buffered saline (pbs)/product/Seikagaku corporation
Average 90 stars, based on 1 article reviews
phosphate buffered saline (pbs) - by Bioz Stars, 2026-03
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ni-nta binding buffer (20 mm tris at ph 8.0, 1 m nacl, 500 mm urea, 25 mm imidazole, 10 mm β-mercaptoethanol)  (AVESTIN Inc)
90
AVESTIN Inc ni-nta binding buffer (20 mm tris at ph 8.0, 1 m nacl, 500 mm urea, 25 mm imidazole, 10 mm β-mercaptoethanol)
Ni Nta Binding Buffer (20 Mm Tris At Ph 8.0, 1 M Nacl, 500 Mm Urea, 25 Mm Imidazole, 10 Mm β Mercaptoethanol), supplied by AVESTIN Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ni-nta binding buffer (20 mm tris at ph 8.0, 1 m nacl, 500 mm urea, 25 mm imidazole, 10 mm β-mercaptoethanol)/product/AVESTIN Inc
Average 90 stars, based on 1 article reviews
ni-nta binding buffer (20 mm tris at ph 8.0, 1 m nacl, 500 mm urea, 25 mm imidazole, 10 mm β-mercaptoethanol) - by Bioz Stars, 2026-03
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lysis buffer (50 tris ph 8, nacl, 5% glycerol, 2-mercaptoethanol)  (BioShop)
90
BioShop lysis buffer (50 tris ph 8, nacl, 5% glycerol, 2-mercaptoethanol)
Lysis Buffer (50 Tris Ph 8, Nacl, 5% Glycerol, 2 Mercaptoethanol), supplied by BioShop, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/lysis buffer (50 tris ph 8, nacl, 5% glycerol, 2-mercaptoethanol)/product/BioShop
Average 90 stars, based on 1 article reviews
lysis buffer (50 tris ph 8, nacl, 5% glycerol, 2-mercaptoethanol) - by Bioz Stars, 2026-03
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150 mm phosphate buffer (ph 6.0) containing 500 mm nacl  (Diagnostica Stago)
90
Diagnostica Stago 150 mm phosphate buffer (ph 6.0) containing 500 mm nacl
150 Mm Phosphate Buffer (Ph 6.0) Containing 500 Mm Nacl, supplied by Diagnostica Stago, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/150 mm phosphate buffer (ph 6.0) containing 500 mm nacl/product/Diagnostica Stago
Average 90 stars, based on 1 article reviews
150 mm phosphate buffer (ph 6.0) containing 500 mm nacl - by Bioz Stars, 2026-03
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escn-esco buffer (20 mm hepes, ph 7.5, 500 mm nacl, 5% glycerol, 0.5 mm tcep-hcl)  (Haematologic Technologies)
90
Haematologic Technologies escn-esco buffer (20 mm hepes, ph 7.5, 500 mm nacl, 5% glycerol, 0.5 mm tcep-hcl)
Cryo-EM density and resolution. Cryo-EM maps, coloured by subunit, of the a class one reconstruction comprising the <t>EscN</t> hexamer (without visible <t>EscO</t> density) at 3.34 Å resolution, and of the d class two reconstruction of the EscN-EscO complex at 3.29 Å resolution. Representative density is shown for b class one (EscN chain C residues 238–258 and 290–311) contoured at 6 σ and e class two (EscO residues 1–19 and 103–122) contoured at 4 σ . c Sample density of the class two catalytic site ligands ADP, AlF 3 (grey and cyan), and Mg 2+ (green), contoured at 4 σ . Ligand coordination is represented with dotted lines, while the curved lines demarcate the reaction mechanism
Escn Esco Buffer (20 Mm Hepes, Ph 7.5, 500 Mm Nacl, 5% Glycerol, 0.5 Mm Tcep Hcl), supplied by Haematologic Technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/escn-esco buffer (20 mm hepes, ph 7.5, 500 mm nacl, 5% glycerol, 0.5 mm tcep-hcl)/product/Haematologic Technologies
Average 90 stars, based on 1 article reviews
escn-esco buffer (20 mm hepes, ph 7.5, 500 mm nacl, 5% glycerol, 0.5 mm tcep-hcl) - by Bioz Stars, 2026-03
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buffer a (50 ml 1× phosphate-buffered saline (pbs), 500 mm nacl, 20 mm imidazole)  (Microfluidics Inc)
90
Microfluidics Inc buffer a (50 ml 1× phosphate-buffered saline (pbs), 500 mm nacl, 20 mm imidazole)
Cryo-EM density and resolution. Cryo-EM maps, coloured by subunit, of the a class one reconstruction comprising the <t>EscN</t> hexamer (without visible <t>EscO</t> density) at 3.34 Å resolution, and of the d class two reconstruction of the EscN-EscO complex at 3.29 Å resolution. Representative density is shown for b class one (EscN chain C residues 238–258 and 290–311) contoured at 6 σ and e class two (EscO residues 1–19 and 103–122) contoured at 4 σ . c Sample density of the class two catalytic site ligands ADP, AlF 3 (grey and cyan), and Mg 2+ (green), contoured at 4 σ . Ligand coordination is represented with dotted lines, while the curved lines demarcate the reaction mechanism
Buffer A (50 Ml 1× Phosphate Buffered Saline (Pbs), 500 Mm Nacl, 20 Mm Imidazole), supplied by Microfluidics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/buffer a (50 ml 1× phosphate-buffered saline (pbs), 500 mm nacl, 20 mm imidazole)/product/Microfluidics Inc
Average 90 stars, based on 1 article reviews
buffer a (50 ml 1× phosphate-buffered saline (pbs), 500 mm nacl, 20 mm imidazole) - by Bioz Stars, 2026-03
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human α-thrombin, mm 36,500 d, 3010 nih u/mg activity in ph 6.5, 0.05 m sodium citrate buffer, 0.2 m nacl, 0.1% peg-8000  (Enzyme Research Laboratories)
90
Enzyme Research Laboratories human α-thrombin, mm 36,500 d, 3010 nih u/mg activity in ph 6.5, 0.05 m sodium citrate buffer, 0.2 m nacl, 0.1% peg-8000
Cryo-EM density and resolution. Cryo-EM maps, coloured by subunit, of the a class one reconstruction comprising the <t>EscN</t> hexamer (without visible <t>EscO</t> density) at 3.34 Å resolution, and of the d class two reconstruction of the EscN-EscO complex at 3.29 Å resolution. Representative density is shown for b class one (EscN chain C residues 238–258 and 290–311) contoured at 6 σ and e class two (EscO residues 1–19 and 103–122) contoured at 4 σ . c Sample density of the class two catalytic site ligands ADP, AlF 3 (grey and cyan), and Mg 2+ (green), contoured at 4 σ . Ligand coordination is represented with dotted lines, while the curved lines demarcate the reaction mechanism
Human α Thrombin, Mm 36,500 D, 3010 Nih U/Mg Activity In Ph 6.5, 0.05 M Sodium Citrate Buffer, 0.2 M Nacl, 0.1% Peg 8000, supplied by Enzyme Research Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/human α-thrombin, mm 36,500 d, 3010 nih u/mg activity in ph 6.5, 0.05 m sodium citrate buffer, 0.2 m nacl, 0.1% peg-8000/product/Enzyme Research Laboratories
Average 90 stars, based on 1 article reviews
human α-thrombin, mm 36,500 d, 3010 nih u/mg activity in ph 6.5, 0.05 m sodium citrate buffer, 0.2 m nacl, 0.1% peg-8000 - by Bioz Stars, 2026-03
90/100 stars
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lyses buffer consisting of 20 mm sodium phosphate (ph 8.0), 500 mm nacl, and 1x protease inhibitor  (ApexBio)
90
ApexBio lyses buffer consisting of 20 mm sodium phosphate (ph 8.0), 500 mm nacl, and 1x protease inhibitor
Cryo-EM density and resolution. Cryo-EM maps, coloured by subunit, of the a class one reconstruction comprising the <t>EscN</t> hexamer (without visible <t>EscO</t> density) at 3.34 Å resolution, and of the d class two reconstruction of the EscN-EscO complex at 3.29 Å resolution. Representative density is shown for b class one (EscN chain C residues 238–258 and 290–311) contoured at 6 σ and e class two (EscO residues 1–19 and 103–122) contoured at 4 σ . c Sample density of the class two catalytic site ligands ADP, AlF 3 (grey and cyan), and Mg 2+ (green), contoured at 4 σ . Ligand coordination is represented with dotted lines, while the curved lines demarcate the reaction mechanism
Lyses Buffer Consisting Of 20 Mm Sodium Phosphate (Ph 8.0), 500 Mm Nacl, And 1x Protease Inhibitor, supplied by ApexBio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/lyses buffer consisting of 20 mm sodium phosphate (ph 8.0), 500 mm nacl, and 1x protease inhibitor/product/ApexBio
Average 90 stars, based on 1 article reviews
lyses buffer consisting of 20 mm sodium phosphate (ph 8.0), 500 mm nacl, and 1x protease inhibitor - by Bioz Stars, 2026-03
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nickel-binding buffer (25 mm tris-hcl, ph 7.4, 500 mm nacl, 20 mm imidazole)  (Merck KGaA)
90
Merck KGaA nickel-binding buffer (25 mm tris-hcl, ph 7.4, 500 mm nacl, 20 mm imidazole)
Cryo-EM density and resolution. Cryo-EM maps, coloured by subunit, of the a class one reconstruction comprising the <t>EscN</t> hexamer (without visible <t>EscO</t> density) at 3.34 Å resolution, and of the d class two reconstruction of the EscN-EscO complex at 3.29 Å resolution. Representative density is shown for b class one (EscN chain C residues 238–258 and 290–311) contoured at 6 σ and e class two (EscO residues 1–19 and 103–122) contoured at 4 σ . c Sample density of the class two catalytic site ligands ADP, AlF 3 (grey and cyan), and Mg 2+ (green), contoured at 4 σ . Ligand coordination is represented with dotted lines, while the curved lines demarcate the reaction mechanism
Nickel Binding Buffer (25 Mm Tris Hcl, Ph 7.4, 500 Mm Nacl, 20 Mm Imidazole), 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
https://www.bioz.com/result/nickel-binding buffer (25 mm tris-hcl, ph 7.4, 500 mm nacl, 20 mm imidazole)/product/Merck KGaA
Average 90 stars, based on 1 article reviews
nickel-binding buffer (25 mm tris-hcl, ph 7.4, 500 mm nacl, 20 mm imidazole) - by Bioz Stars, 2026-03
90/100 stars
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Image Search Results


Cryo-EM density and resolution. Cryo-EM maps, coloured by subunit, of the a class one reconstruction comprising the EscN hexamer (without visible EscO density) at 3.34 Å resolution, and of the d class two reconstruction of the EscN-EscO complex at 3.29 Å resolution. Representative density is shown for b class one (EscN chain C residues 238–258 and 290–311) contoured at 6 σ and e class two (EscO residues 1–19 and 103–122) contoured at 4 σ . c Sample density of the class two catalytic site ligands ADP, AlF 3 (grey and cyan), and Mg 2+ (green), contoured at 4 σ . Ligand coordination is represented with dotted lines, while the curved lines demarcate the reaction mechanism

Journal: Nature Communications

Article Title: Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry

doi: 10.1038/s41467-019-08477-7

Figure Lengend Snippet: Cryo-EM density and resolution. Cryo-EM maps, coloured by subunit, of the a class one reconstruction comprising the EscN hexamer (without visible EscO density) at 3.34 Å resolution, and of the d class two reconstruction of the EscN-EscO complex at 3.29 Å resolution. Representative density is shown for b class one (EscN chain C residues 238–258 and 290–311) contoured at 6 σ and e class two (EscO residues 1–19 and 103–122) contoured at 4 σ . c Sample density of the class two catalytic site ligands ADP, AlF 3 (grey and cyan), and Mg 2+ (green), contoured at 4 σ . Ligand coordination is represented with dotted lines, while the curved lines demarcate the reaction mechanism

Article Snippet: To remove the his-tag, the proteins were desalted into EscN-EscO buffer (20 mM HEPES, pH 7.5, 500 mM NaCl, 5% glycerol, 0.5 mM TCEP-HCl) and incubated with bovine α-thrombin (Haematologic Technologies Incorporated) at 4 °C overnight at a molar ratio of 1:1000.

Techniques: Cryo-EM Sample Prep

Overview of EscN-EscO complex. a Sphere representation of the EscN-EscO complex (class 2), coloured by subunit and shown from an angled view and side view to highlight the cleft (located between the light and dark green subunits). The EscO stalk (orange) tilts towards the cleft. b Top view of EscN-EscO complex, with negatively charged glutamates shown in red lining the pore, compared with the APBS-calculated electrostatic surface demonstrating the complementary charges of EscN (red, white, blue) and EscO (pink, white, light blue). c Stick depiction of EscO insertion into the EscN pore, where it penetrates ~30 Å; the F 1 γ-subunit (PDB 1H8E) is overlaid in white, demonstrating its longer ~70 Å extension into the F 1 ATPase pore. EscN Glu401 lining the pore is represented as yellow spheres. d EscO coloured by hydrophobicity, with hydrophobic residues coloured yellow and hydrophilic residues coloured teal; hydrophobic residues line the coiled coil interface, characteristic of this motif

Journal: Nature Communications

Article Title: Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry

doi: 10.1038/s41467-019-08477-7

Figure Lengend Snippet: Overview of EscN-EscO complex. a Sphere representation of the EscN-EscO complex (class 2), coloured by subunit and shown from an angled view and side view to highlight the cleft (located between the light and dark green subunits). The EscO stalk (orange) tilts towards the cleft. b Top view of EscN-EscO complex, with negatively charged glutamates shown in red lining the pore, compared with the APBS-calculated electrostatic surface demonstrating the complementary charges of EscN (red, white, blue) and EscO (pink, white, light blue). c Stick depiction of EscO insertion into the EscN pore, where it penetrates ~30 Å; the F 1 γ-subunit (PDB 1H8E) is overlaid in white, demonstrating its longer ~70 Å extension into the F 1 ATPase pore. EscN Glu401 lining the pore is represented as yellow spheres. d EscO coloured by hydrophobicity, with hydrophobic residues coloured yellow and hydrophilic residues coloured teal; hydrophobic residues line the coiled coil interface, characteristic of this motif

Article Snippet: To remove the his-tag, the proteins were desalted into EscN-EscO buffer (20 mM HEPES, pH 7.5, 500 mM NaCl, 5% glycerol, 0.5 mM TCEP-HCl) and incubated with bovine α-thrombin (Haematologic Technologies Incorporated) at 4 °C overnight at a molar ratio of 1:1000.

Techniques:

Characterized EscN/EscO mutants. Side-chain views of previously studied EscN mutants (shown in orange) mapped to the model, as well as EscN mutants (grey) and EscO mutants (yellow) characterized in this paper. The central view of the T and T′ interface provides context for the location of each site, with detailed stick views denoting side-chain locations in the a chaperone binding site, b EscN-EscO interaction interface, c active site and d hydrophobic oligomerization interface

Journal: Nature Communications

Article Title: Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry

doi: 10.1038/s41467-019-08477-7

Figure Lengend Snippet: Characterized EscN/EscO mutants. Side-chain views of previously studied EscN mutants (shown in orange) mapped to the model, as well as EscN mutants (grey) and EscO mutants (yellow) characterized in this paper. The central view of the T and T′ interface provides context for the location of each site, with detailed stick views denoting side-chain locations in the a chaperone binding site, b EscN-EscO interaction interface, c active site and d hydrophobic oligomerization interface

Article Snippet: To remove the his-tag, the proteins were desalted into EscN-EscO buffer (20 mM HEPES, pH 7.5, 500 mM NaCl, 5% glycerol, 0.5 mM TCEP-HCl) and incubated with bovine α-thrombin (Haematologic Technologies Incorporated) at 4 °C overnight at a molar ratio of 1:1000.

Techniques: Binding Assay

EscN catalysis. a Top view of EscN homohexamer without EscO compared to F 1 (1E1R) and V 1 (3VR6) heterohexamers, with subunit names labelled along the periphery; nucleotides are shown as orange spheres. b Comparison of the EscN inter-site distances for all four nucleotide-bound sites, with Cα distances between Ser184 and Arg366 progressively decreasing from 11.9, 11.2, 11.1, and 10.8 Å through sites T to D′. Overlay of EscN (subunits coloured as in (A)), F 1 -ATPase (coloured tan, 1E1R) and V 1 -ATPase (coloured brown, 3VR6). c T, β TP and A N sites and d D, β DP and A N′ sites, demonstrating the similarities in side-chain residues and water positions. Blue density is carved around Mg 2+ and waters from a class 2 map ( B -factor sharpened by a factor of −150 and contoured at 10 σ ), showing the broad density that encompasses the coordinating waters. e Possible rotational catalysis mechanism of EscN and EscO, with the central arrow representing the direction of EscO’s tilt

Journal: Nature Communications

Article Title: Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry

doi: 10.1038/s41467-019-08477-7

Figure Lengend Snippet: EscN catalysis. a Top view of EscN homohexamer without EscO compared to F 1 (1E1R) and V 1 (3VR6) heterohexamers, with subunit names labelled along the periphery; nucleotides are shown as orange spheres. b Comparison of the EscN inter-site distances for all four nucleotide-bound sites, with Cα distances between Ser184 and Arg366 progressively decreasing from 11.9, 11.2, 11.1, and 10.8 Å through sites T to D′. Overlay of EscN (subunits coloured as in (A)), F 1 -ATPase (coloured tan, 1E1R) and V 1 -ATPase (coloured brown, 3VR6). c T, β TP and A N sites and d D, β DP and A N′ sites, demonstrating the similarities in side-chain residues and water positions. Blue density is carved around Mg 2+ and waters from a class 2 map ( B -factor sharpened by a factor of −150 and contoured at 10 σ ), showing the broad density that encompasses the coordinating waters. e Possible rotational catalysis mechanism of EscN and EscO, with the central arrow representing the direction of EscO’s tilt

Article Snippet: To remove the his-tag, the proteins were desalted into EscN-EscO buffer (20 mM HEPES, pH 7.5, 500 mM NaCl, 5% glycerol, 0.5 mM TCEP-HCl) and incubated with bovine α-thrombin (Haematologic Technologies Incorporated) at 4 °C overnight at a molar ratio of 1:1000.

Techniques:

Function of EscN-EscO in the injectisome. a Overview of EscN and EscV location in the context of the T3SS nanomachine (based on in situ tomography of the Salmonella injectisome, EMDB 8544). b Putative binding sites of type III chaperone-substrate complexes, based on previous studies on SrcA/SsaN and CesA/EspA/EscV. Each binding site brings the cargo into the lumen between EscN and EscV. The unresolved region of EscO is represented by a dotted line. c Schematic of proteins present in the cytoplasmic subcomplex. It has been hypothesized that the entire ATPase complex may rise towards the inner membrane to interact with the export gate

Journal: Nature Communications

Article Title: Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry

doi: 10.1038/s41467-019-08477-7

Figure Lengend Snippet: Function of EscN-EscO in the injectisome. a Overview of EscN and EscV location in the context of the T3SS nanomachine (based on in situ tomography of the Salmonella injectisome, EMDB 8544). b Putative binding sites of type III chaperone-substrate complexes, based on previous studies on SrcA/SsaN and CesA/EspA/EscV. Each binding site brings the cargo into the lumen between EscN and EscV. The unresolved region of EscO is represented by a dotted line. c Schematic of proteins present in the cytoplasmic subcomplex. It has been hypothesized that the entire ATPase complex may rise towards the inner membrane to interact with the export gate

Article Snippet: To remove the his-tag, the proteins were desalted into EscN-EscO buffer (20 mM HEPES, pH 7.5, 500 mM NaCl, 5% glycerol, 0.5 mM TCEP-HCl) and incubated with bovine α-thrombin (Haematologic Technologies Incorporated) at 4 °C overnight at a molar ratio of 1:1000.

Techniques: In Situ, Tomography, Binding Assay