pumilus  (ATCC)


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    Structured Review

    ATCC pumilus
    Homologous recombination in B . <t>pumilus</t> C1 using p3022. The hybrid plasmid p3022 was made by cloning p3019 into the Xba I and Pst I sites of pE194. This plasmid was designed to be used as a temperature-sensitive shuttle plasmid for Bacillus and E . coli . The bla gene encodes ampicillin resistance for selection in E . coli , and ermC encodes erythromycin resistance for selection in Bacillus . The cynD 539 encodes the partial 539-bp PCR product from the putative cyanide dihydratase of B . pumilus C1. B . pumilus C1 was transformed with p3022 to make strain MB3025. This diagram shows p3022 integration into the cyanide dihydratase gene of B . pumilus C1 by homologous recombination. (A) Recognition of homologous regions of p3022 with the gene encoding cyanide dihydratase. (B) The integrated plasmid p3022 flanked by the gene encoding cyanide dihydratase. The gene encoding replication initiation protein for plasmid replication in Bacillus species, repF , is also shown. The origin of plus-strand synthesis, ori + , is not shown but is located within the repF gene.
    Pumilus, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pumilus/product/ATCC
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pumilus - by Bioz Stars, 2022-10
    94/100 stars

    Images

    1) Product Images from "CynD, the Cyanide Dihydratase from Bacillus pumilus: Gene Cloning and Structural Studies"

    Article Title: CynD, the Cyanide Dihydratase from Bacillus pumilus: Gene Cloning and Structural Studies

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.69.8.4794-4805.2003

    Homologous recombination in B . pumilus C1 using p3022. The hybrid plasmid p3022 was made by cloning p3019 into the Xba I and Pst I sites of pE194. This plasmid was designed to be used as a temperature-sensitive shuttle plasmid for Bacillus and E . coli . The bla gene encodes ampicillin resistance for selection in E . coli , and ermC encodes erythromycin resistance for selection in Bacillus . The cynD 539 encodes the partial 539-bp PCR product from the putative cyanide dihydratase of B . pumilus C1. B . pumilus C1 was transformed with p3022 to make strain MB3025. This diagram shows p3022 integration into the cyanide dihydratase gene of B . pumilus C1 by homologous recombination. (A) Recognition of homologous regions of p3022 with the gene encoding cyanide dihydratase. (B) The integrated plasmid p3022 flanked by the gene encoding cyanide dihydratase. The gene encoding replication initiation protein for plasmid replication in Bacillus species, repF , is also shown. The origin of plus-strand synthesis, ori + , is not shown but is located within the repF gene.
    Figure Legend Snippet: Homologous recombination in B . pumilus C1 using p3022. The hybrid plasmid p3022 was made by cloning p3019 into the Xba I and Pst I sites of pE194. This plasmid was designed to be used as a temperature-sensitive shuttle plasmid for Bacillus and E . coli . The bla gene encodes ampicillin resistance for selection in E . coli , and ermC encodes erythromycin resistance for selection in Bacillus . The cynD 539 encodes the partial 539-bp PCR product from the putative cyanide dihydratase of B . pumilus C1. B . pumilus C1 was transformed with p3022 to make strain MB3025. This diagram shows p3022 integration into the cyanide dihydratase gene of B . pumilus C1 by homologous recombination. (A) Recognition of homologous regions of p3022 with the gene encoding cyanide dihydratase. (B) The integrated plasmid p3022 flanked by the gene encoding cyanide dihydratase. The gene encoding replication initiation protein for plasmid replication in Bacillus species, repF , is also shown. The origin of plus-strand synthesis, ori + , is not shown but is located within the repF gene.

    Techniques Used: Homologous Recombination, Plasmid Preparation, Clone Assay, Selection, Polymerase Chain Reaction, Transformation Assay

    Three-dimensional reconstruction of negatively stained micrographs of the cyanide dihydratase from B . pumilus at a resolution of 3.2 nm. Shown are the views down the twofold axis (A and C) and a view perpendicular to the twofold axis (B). The structure is a spiral of two turns from end to end, having 18 subunits.
    Figure Legend Snippet: Three-dimensional reconstruction of negatively stained micrographs of the cyanide dihydratase from B . pumilus at a resolution of 3.2 nm. Shown are the views down the twofold axis (A and C) and a view perpendicular to the twofold axis (B). The structure is a spiral of two turns from end to end, having 18 subunits.

    Techniques Used: Staining

    Negative-stain electron micrographs of the isolated cyanide dihydratase from B . pumilus at pH 8.0 (A) and 5.4 (B) illustrating the transition from discrete particles to extended rods. (C) Platinum-carbon shadowing of the cyanide dihydratase rods. Regular striations along the length of the rod can be seen in rods lying parallel to the direction of shadowing. The angle of the striations implies that the helical arrangement of subunits is left handed. The location of five of the striations is emphasized by white lines.
    Figure Legend Snippet: Negative-stain electron micrographs of the isolated cyanide dihydratase from B . pumilus at pH 8.0 (A) and 5.4 (B) illustrating the transition from discrete particles to extended rods. (C) Platinum-carbon shadowing of the cyanide dihydratase rods. Regular striations along the length of the rod can be seen in rods lying parallel to the direction of shadowing. The angle of the striations implies that the helical arrangement of subunits is left handed. The location of five of the striations is emphasized by white lines.

    Techniques Used: Staining, Isolation

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    ATCC b pumilus atcc 7061
    Genetics and enzymology of PZN biosynthesis. (a) The 10 kb PZN biosynthetic gene cluster from Bacillus amyloliquefaciens FZB42. (b) The precursor peptides for PZN and potential analogs from other species exhibit remarkable similarity. Bam, B. amyloliquefaciens FZB42; Bpum, B. <t>pumilus</t> ATCC 7061; Cms, Clavibacter michiganensis subsp. sepedonicus ; Cur, Corynebacterium urealyticum DSM 7109; Blin, Brevibacterium linens BL2. Color-coding (predicted for Cms, Cur, and Blin): green, N α ,N α -dimethylarginine; red, thiazoles; blue (methyl)oxazoles; brown, methyloxazoline; *, peptidase cleavage site. (c) Posttranslational modification of cysteine, serine, and threonine residues in TOMM biosynthesis proceeds by cyclodehydration (mass loss of 18 Da) and subsequent oxidation (additional mass loss of 2 Da). (d) The chemical structure of PZN. Color-coding is identical to panel b.
    B Pumilus Atcc 7061, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Genetics and enzymology of PZN biosynthesis. (a) The 10 kb PZN biosynthetic gene cluster from Bacillus amyloliquefaciens FZB42. (b) The precursor peptides for PZN and potential analogs from other species exhibit remarkable similarity. Bam, B. amyloliquefaciens FZB42; Bpum, B. pumilus ATCC 7061; Cms, Clavibacter michiganensis subsp. sepedonicus ; Cur, Corynebacterium urealyticum DSM 7109; Blin, Brevibacterium linens BL2. Color-coding (predicted for Cms, Cur, and Blin): green, N α ,N α -dimethylarginine; red, thiazoles; blue (methyl)oxazoles; brown, methyloxazoline; *, peptidase cleavage site. (c) Posttranslational modification of cysteine, serine, and threonine residues in TOMM biosynthesis proceeds by cyclodehydration (mass loss of 18 Da) and subsequent oxidation (additional mass loss of 2 Da). (d) The chemical structure of PZN. Color-coding is identical to panel b.

    Journal: ACS chemical biology

    Article Title: Engineering unnatural variants of plantazolicin through codon reprogramming

    doi: 10.1021/cb4003392

    Figure Lengend Snippet: Genetics and enzymology of PZN biosynthesis. (a) The 10 kb PZN biosynthetic gene cluster from Bacillus amyloliquefaciens FZB42. (b) The precursor peptides for PZN and potential analogs from other species exhibit remarkable similarity. Bam, B. amyloliquefaciens FZB42; Bpum, B. pumilus ATCC 7061; Cms, Clavibacter michiganensis subsp. sepedonicus ; Cur, Corynebacterium urealyticum DSM 7109; Blin, Brevibacterium linens BL2. Color-coding (predicted for Cms, Cur, and Blin): green, N α ,N α -dimethylarginine; red, thiazoles; blue (methyl)oxazoles; brown, methyloxazoline; *, peptidase cleavage site. (c) Posttranslational modification of cysteine, serine, and threonine residues in TOMM biosynthesis proceeds by cyclodehydration (mass loss of 18 Da) and subsequent oxidation (additional mass loss of 2 Da). (d) The chemical structure of PZN. Color-coding is identical to panel b.

    Article Snippet: The amino acid sequences of the core peptides from B. pumilus ATCC 7061 and B. amyloliquefaciens FZB42 are identical ( ) , rendering it necessary to look to the other potential PZN producers in order to determine if E. coli could biosynthesize non- Bacillus PZN compounds.

    Techniques: Modification

    Viability of SAFR-032 spores (5.63 × 10 8 ) after 1 h of exposure to 5% hydrogen peroxide. The bars represent means of three replicates, and the error bars represent the standard deviations. Bars: 1, untreated control (standard deviation [SD], ±1.2 × 10 8 ); 2, treatment with 5% H 2 O 2 (SD, ±5.6 × 10 5 ); 3, control treated with 0.1 mM NH 2 OH (SD, ±1.3 × 10 8 ); 4, treatment with 0.1 mM NH 2 OH for 10 min before exposure to 5% H 2 O 2 (SD, ±7 × 10 3 ).

    Journal: Applied and Environmental Microbiology

    Article Title: Protection of Bacillus pumilus Spores by Catalases

    doi: 10.1128/AEM.01211-12

    Figure Lengend Snippet: Viability of SAFR-032 spores (5.63 × 10 8 ) after 1 h of exposure to 5% hydrogen peroxide. The bars represent means of three replicates, and the error bars represent the standard deviations. Bars: 1, untreated control (standard deviation [SD], ±1.2 × 10 8 ); 2, treatment with 5% H 2 O 2 (SD, ±5.6 × 10 5 ); 3, control treated with 0.1 mM NH 2 OH (SD, ±1.3 × 10 8 ); 4, treatment with 0.1 mM NH 2 OH for 10 min before exposure to 5% H 2 O 2 (SD, ±7 × 10 3 ).

    Article Snippet: YjqC was very abundant in SAFR-032 spore protein extract but was not present in that of ATCC 7061 ( ).

    Techniques: Standard Deviation

    SDS-PAGE analysis of proteins extracted from intact and decoated B. pumilus spores. Lanes: ST, molecular mass standards (sizes in kDa are on the left); 1, SAFR-032; 2, ATCC 7061; 1A and 2A, intact spore protein extracts; 1B and 2B, decoated spore protein extracts; 1C and 2C, coat protein extracts. Lanes 1A and 1B were cut into ∼1.5-mm slices from the bottom to the top for protein identification by LC-MS/MS. A similar amount of protein (∼10 μg) was loaded into each well. The black arrowheads indicate a sporulation-related manganese catalase (YjqC). The white arrowheads indicate the second manganese catalase (BPUM_1305). The numbers indicate the excised PAGE bands.

    Journal: Applied and Environmental Microbiology

    Article Title: Protection of Bacillus pumilus Spores by Catalases

    doi: 10.1128/AEM.01211-12

    Figure Lengend Snippet: SDS-PAGE analysis of proteins extracted from intact and decoated B. pumilus spores. Lanes: ST, molecular mass standards (sizes in kDa are on the left); 1, SAFR-032; 2, ATCC 7061; 1A and 2A, intact spore protein extracts; 1B and 2B, decoated spore protein extracts; 1C and 2C, coat protein extracts. Lanes 1A and 1B were cut into ∼1.5-mm slices from the bottom to the top for protein identification by LC-MS/MS. A similar amount of protein (∼10 μg) was loaded into each well. The black arrowheads indicate a sporulation-related manganese catalase (YjqC). The white arrowheads indicate the second manganese catalase (BPUM_1305). The numbers indicate the excised PAGE bands.

    Article Snippet: YjqC was very abundant in SAFR-032 spore protein extract but was not present in that of ATCC 7061 ( ).

    Techniques: SDS Page, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Polyacrylamide Gel Electrophoresis

    Spores of B. pumilus SAFR-032 visualized by scanning electron microscopy after treatment with H 2 O 2 . In order to preserve oxygen vesicles, the reaction was performed in 2% albumin and a freezer substitution solvent replacement procedure (acetone containing 5% glutaraldehyde) was used after the rapid freezing of samples in liquid nitrogen. Shown are control spores (magnifications: A, ×20,000; C, ×50,000) and spores treated with H 2 O 2 (magnifications: B, ×20,000; D, ×50,000; E, ×60,000; F, ×110,000). The white arrows indicate oxygen gas vesicles fixed on the spore surface during hydrogen peroxide treatment. The spores in sample E were suspended in water, treated with H 2 O 2 , and freeze-dried; no albumin or glutaraldehyde was used. Panel E provides evidence that treatment with H 2 O 2 causes part of the spore surface to be dislodged and that the resulting membrane fragments bind spores together.

    Journal: Applied and Environmental Microbiology

    Article Title: Protection of Bacillus pumilus Spores by Catalases

    doi: 10.1128/AEM.01211-12

    Figure Lengend Snippet: Spores of B. pumilus SAFR-032 visualized by scanning electron microscopy after treatment with H 2 O 2 . In order to preserve oxygen vesicles, the reaction was performed in 2% albumin and a freezer substitution solvent replacement procedure (acetone containing 5% glutaraldehyde) was used after the rapid freezing of samples in liquid nitrogen. Shown are control spores (magnifications: A, ×20,000; C, ×50,000) and spores treated with H 2 O 2 (magnifications: B, ×20,000; D, ×50,000; E, ×60,000; F, ×110,000). The white arrows indicate oxygen gas vesicles fixed on the spore surface during hydrogen peroxide treatment. The spores in sample E were suspended in water, treated with H 2 O 2 , and freeze-dried; no albumin or glutaraldehyde was used. Panel E provides evidence that treatment with H 2 O 2 causes part of the spore surface to be dislodged and that the resulting membrane fragments bind spores together.

    Article Snippet: YjqC was very abundant in SAFR-032 spore protein extract but was not present in that of ATCC 7061 ( ).

    Techniques: Electron Microscopy

    Thermal activity and stability of the protease produced by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Journal: Brazilian Journal of Microbiology

    Article Title: Optimization and characterization of alkaline protease and carboxymethyl-cellulase produced by Bacillus pumillus grown on Ficus nitida wastes

    doi: 10.1590/S1517-83822013005000048

    Figure Lengend Snippet: Thermal activity and stability of the protease produced by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Article Snippet: Tests on cotton fabric Cotton fabric sample (1.5 g) was incubated at room temperature with 50 mL CMCase of Bacillus pumilus ATCC 7061.

    Techniques: Activity Assay, Produced, Standard Deviation

    Effect of different pH values on the production of protease and CMCase by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Journal: Brazilian Journal of Microbiology

    Article Title: Optimization and characterization of alkaline protease and carboxymethyl-cellulase produced by Bacillus pumillus grown on Ficus nitida wastes

    doi: 10.1590/S1517-83822013005000048

    Figure Lengend Snippet: Effect of different pH values on the production of protease and CMCase by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Article Snippet: Tests on cotton fabric Cotton fabric sample (1.5 g) was incubated at room temperature with 50 mL CMCase of Bacillus pumilus ATCC 7061.

    Techniques: Standard Deviation

    Effect of different incubation period on growth and the production of protease (A), growth and the production of CMCase (B) by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Journal: Brazilian Journal of Microbiology

    Article Title: Optimization and characterization of alkaline protease and carboxymethyl-cellulase produced by Bacillus pumillus grown on Ficus nitida wastes

    doi: 10.1590/S1517-83822013005000048

    Figure Lengend Snippet: Effect of different incubation period on growth and the production of protease (A), growth and the production of CMCase (B) by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Article Snippet: Tests on cotton fabric Cotton fabric sample (1.5 g) was incubated at room temperature with 50 mL CMCase of Bacillus pumilus ATCC 7061.

    Techniques: Incubation, Standard Deviation

    Effect of different nitrogen sources on the production of protease and CMCase by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Journal: Brazilian Journal of Microbiology

    Article Title: Optimization and characterization of alkaline protease and carboxymethyl-cellulase produced by Bacillus pumillus grown on Ficus nitida wastes

    doi: 10.1590/S1517-83822013005000048

    Figure Lengend Snippet: Effect of different nitrogen sources on the production of protease and CMCase by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Article Snippet: Tests on cotton fabric Cotton fabric sample (1.5 g) was incubated at room temperature with 50 mL CMCase of Bacillus pumilus ATCC 7061.

    Techniques: Standard Deviation

    Thermal activity and stability of CMCase produced by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Journal: Brazilian Journal of Microbiology

    Article Title: Optimization and characterization of alkaline protease and carboxymethyl-cellulase produced by Bacillus pumillus grown on Ficus nitida wastes

    doi: 10.1590/S1517-83822013005000048

    Figure Lengend Snippet: Thermal activity and stability of CMCase produced by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Article Snippet: Tests on cotton fabric Cotton fabric sample (1.5 g) was incubated at room temperature with 50 mL CMCase of Bacillus pumilus ATCC 7061.

    Techniques: Activity Assay, Produced, Standard Deviation

    Effect of incubation temperature on the production of protease and CMCase by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Journal: Brazilian Journal of Microbiology

    Article Title: Optimization and characterization of alkaline protease and carboxymethyl-cellulase produced by Bacillus pumillus grown on Ficus nitida wastes

    doi: 10.1590/S1517-83822013005000048

    Figure Lengend Snippet: Effect of incubation temperature on the production of protease and CMCase by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Article Snippet: Tests on cotton fabric Cotton fabric sample (1.5 g) was incubated at room temperature with 50 mL CMCase of Bacillus pumilus ATCC 7061.

    Techniques: Incubation, Standard Deviation

    Effect of different concentrations of Ficus nitida leaves on the production of protease and CMCase by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Journal: Brazilian Journal of Microbiology

    Article Title: Optimization and characterization of alkaline protease and carboxymethyl-cellulase produced by Bacillus pumillus grown on Ficus nitida wastes

    doi: 10.1590/S1517-83822013005000048

    Figure Lengend Snippet: Effect of different concentrations of Ficus nitida leaves on the production of protease and CMCase by Bacillus pumilus ATCC 7061. Results are means of three independent determinations. Bars correspond to standard deviation.

    Article Snippet: Tests on cotton fabric Cotton fabric sample (1.5 g) was incubated at room temperature with 50 mL CMCase of Bacillus pumilus ATCC 7061.

    Techniques: Standard Deviation

    Homologous recombination in B . pumilus C1 using p3022. The hybrid plasmid p3022 was made by cloning p3019 into the Xba I and Pst I sites of pE194. This plasmid was designed to be used as a temperature-sensitive shuttle plasmid for Bacillus and E . coli . The bla gene encodes ampicillin resistance for selection in E . coli , and ermC encodes erythromycin resistance for selection in Bacillus . The cynD 539 encodes the partial 539-bp PCR product from the putative cyanide dihydratase of B . pumilus C1. B . pumilus C1 was transformed with p3022 to make strain MB3025. This diagram shows p3022 integration into the cyanide dihydratase gene of B . pumilus C1 by homologous recombination. (A) Recognition of homologous regions of p3022 with the gene encoding cyanide dihydratase. (B) The integrated plasmid p3022 flanked by the gene encoding cyanide dihydratase. The gene encoding replication initiation protein for plasmid replication in Bacillus species, repF , is also shown. The origin of plus-strand synthesis, ori + , is not shown but is located within the repF gene.

    Journal: Applied and Environmental Microbiology

    Article Title: CynD, the Cyanide Dihydratase from Bacillus pumilus: Gene Cloning and Structural Studies

    doi: 10.1128/AEM.69.8.4794-4805.2003

    Figure Lengend Snippet: Homologous recombination in B . pumilus C1 using p3022. The hybrid plasmid p3022 was made by cloning p3019 into the Xba I and Pst I sites of pE194. This plasmid was designed to be used as a temperature-sensitive shuttle plasmid for Bacillus and E . coli . The bla gene encodes ampicillin resistance for selection in E . coli , and ermC encodes erythromycin resistance for selection in Bacillus . The cynD 539 encodes the partial 539-bp PCR product from the putative cyanide dihydratase of B . pumilus C1. B . pumilus C1 was transformed with p3022 to make strain MB3025. This diagram shows p3022 integration into the cyanide dihydratase gene of B . pumilus C1 by homologous recombination. (A) Recognition of homologous regions of p3022 with the gene encoding cyanide dihydratase. (B) The integrated plasmid p3022 flanked by the gene encoding cyanide dihydratase. The gene encoding replication initiation protein for plasmid replication in Bacillus species, repF , is also shown. The origin of plus-strand synthesis, ori + , is not shown but is located within the repF gene.

    Article Snippet: To test this, we attempted to amplify this gene from a wild-type isolate of B . pumilus (Bacillus Genetic Stock Collection BGSC 8A3 or ATCC 7061) with the primers Pum- Nde I and Pum- Xho I.

    Techniques: Homologous Recombination, Plasmid Preparation, Clone Assay, Selection, Polymerase Chain Reaction, Transformation Assay

    Three-dimensional reconstruction of negatively stained micrographs of the cyanide dihydratase from B . pumilus at a resolution of 3.2 nm. Shown are the views down the twofold axis (A and C) and a view perpendicular to the twofold axis (B). The structure is a spiral of two turns from end to end, having 18 subunits.

    Journal: Applied and Environmental Microbiology

    Article Title: CynD, the Cyanide Dihydratase from Bacillus pumilus: Gene Cloning and Structural Studies

    doi: 10.1128/AEM.69.8.4794-4805.2003

    Figure Lengend Snippet: Three-dimensional reconstruction of negatively stained micrographs of the cyanide dihydratase from B . pumilus at a resolution of 3.2 nm. Shown are the views down the twofold axis (A and C) and a view perpendicular to the twofold axis (B). The structure is a spiral of two turns from end to end, having 18 subunits.

    Article Snippet: To test this, we attempted to amplify this gene from a wild-type isolate of B . pumilus (Bacillus Genetic Stock Collection BGSC 8A3 or ATCC 7061) with the primers Pum- Nde I and Pum- Xho I.

    Techniques: Staining

    Negative-stain electron micrographs of the isolated cyanide dihydratase from B . pumilus at pH 8.0 (A) and 5.4 (B) illustrating the transition from discrete particles to extended rods. (C) Platinum-carbon shadowing of the cyanide dihydratase rods. Regular striations along the length of the rod can be seen in rods lying parallel to the direction of shadowing. The angle of the striations implies that the helical arrangement of subunits is left handed. The location of five of the striations is emphasized by white lines.

    Journal: Applied and Environmental Microbiology

    Article Title: CynD, the Cyanide Dihydratase from Bacillus pumilus: Gene Cloning and Structural Studies

    doi: 10.1128/AEM.69.8.4794-4805.2003

    Figure Lengend Snippet: Negative-stain electron micrographs of the isolated cyanide dihydratase from B . pumilus at pH 8.0 (A) and 5.4 (B) illustrating the transition from discrete particles to extended rods. (C) Platinum-carbon shadowing of the cyanide dihydratase rods. Regular striations along the length of the rod can be seen in rods lying parallel to the direction of shadowing. The angle of the striations implies that the helical arrangement of subunits is left handed. The location of five of the striations is emphasized by white lines.

    Article Snippet: To test this, we attempted to amplify this gene from a wild-type isolate of B . pumilus (Bacillus Genetic Stock Collection BGSC 8A3 or ATCC 7061) with the primers Pum- Nde I and Pum- Xho I.

    Techniques: Staining, Isolation