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rp4 plasmid (ATCC)

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ATCC rp4 plasmid
Rp4 Plasmid, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 20065 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rp4+plasmid/Plasmid/pm40945801-177-16-26
Average 99 stars, based on 20065 article reviews

rp4 plasmid - by Bioz Stars, 2026-10

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Plasmid Preparation:

Article Title: Horizontal transfer of the multidrug resistance plasmid RP4 inhibits ammonia nitrogen removal dominated by ammonia-oxidizing bacteria.
Article Snippet: Color micrographs were captured using a camera (Olympus, SP2-BSW, Japan). .. Furthermore, the E. coli K12 Rif (RP4) strain, sludge samples without the RP4 plasmid, and a pure culture of an AOB (Nitrosomonas europaea, ATCC 25,978) were used as controls. ..

Article Title: Horizontal transfer of the multidrug resistance plasmid RP4 inhibits ammonia nitrogen removal dominated by ammonia-oxidizing bacteria.
Article Snippet: .. To achieve this, we established sequencing batch reactors (SBRs) and a conjugation model with E. coli donor strains carrying the RP4 plasmid and a typical ammonia-oxidating (AOB) bacterial strain (Nitrosomonas europaea ATCC 25978) as a recipient to investigate the effect of conjugative transfer of plasmid RP4 on AOB. .. Our findings demonstrated that the RP4 plasmid carried by the donor strains could be transferred to AOB in the SBR and to Nitrosomonas europaea ATCC 25978.

Article Title: Horizontal transfer of the multidrug resistance plasmid RP4 inhibits ammonia nitrogen removal dominated by ammonia-oxidizing bacteria.
Article Snippet: .. Once the RP4 plasmid entered N. europaea ATCC 25978 in the conjugation model, ammonia removal was significantly inhibited and nitrite generation was decreased. ..

Article Title: Multidrug-resistant plasmid modulates ammonia oxidation efficiency in Nitrosomonas europaea through cyclic di-guanylate and acyl-homoserine lactones pathways.
Article Snippet: • The RP4 plasmid increased the concentrations of c-di-GMP and AHLs.. • Increased c-di-GMP levels promote the production of C4-HSL, C6-HSL, and C8-

Article Title: Construction and Characterization of a recA Mutant of Thiobacillus ferrooxidans by Marker Exchange Mutagenesis
Article Snippet: ATCC 33020 Isolated from a uranium mine in Japan ATCCa ATCC 19859 Isolated from acid copper leaching water in Canada ATCC Tf-49 Isolated from a coal mine in Yunqin (China) 24 BRGM1 Isolated twice on DOP medium from the BRGM strain 8 .. HB101 D(gpt-proA)62 leuB6 supE44 ara-14 galK2 lacY1 D(mcr-mrr) rpsL20 xyl-5 mtl-1 recA13 MC1061 araD139 D(ara-leu)7696 galE15 galK16 D(lac)X74 rpsL hsdR2(rK 2 mK 1) mcrA mcrB1 MOS Blue endA1 hsdR17(rK 2 mK 1) supE44 thi1 gyrA46 recA1 lac/F9 (lacIqZDM15 proAB Tn10) S17-1 recA pro hsdR (RP4-2 Tc::Mu Km::Tn7) 31 CGSC7330 pro-81::Tn10 rph-1 E. coli Genetic Stock Center Plasmids pNG23 recA-recX-alaS region cloned in the HindIII site of pUC19; identical to pNG22 (14) with the insert in the opposite orientation pHP45V-Km pHP45 plasmid carrying the V-Km cassette 13 pUC18mob pUC18 plasmid in which an Sau3A fragment carrying the mob region of the RP4 plasmid has been inserted in the BamHI site 31 RP4 Apr Tcr Kmr IncP Tra1 10 pKT240 Apr Kmr (Tn903) IncQ Mob1 4 pJRD215 Smr Kmr (Tn5) IncQ Mob1 11 pJB3Km1 Apr Kmr (Tn903) IncP Mob1 7 pUFR034 Kmr (Tn903) IncW Mob1 12 a ATCC, American Type Culture Collection. on June 14, 2015 by R itsum eikan U niversity http://jb.asm .org/ D ow nloaded from the V-Km cassette had been inserted RECA4 (59-CGGCTCGCTGGGTCTGG39) or ARECA5 (59-CTGACAACTGGCTATGGC-39), and an oligonucleotide corresponding to the end of the V-Km cassette, CKMTN5 (59-GGAGTGGGG AGGCACGATGG-39). ..

Sequencing:

Article Title: Horizontal transfer of the multidrug resistance plasmid RP4 inhibits ammonia nitrogen removal dominated by ammonia-oxidizing bacteria.
Article Snippet: .. To achieve this, we established sequencing batch reactors (SBRs) and a conjugation model with E. coli donor strains carrying the RP4 plasmid and a typical ammonia-oxidating (AOB) bacterial strain (Nitrosomonas europaea ATCC 25978) as a recipient to investigate the effect of conjugative transfer of plasmid RP4 on AOB. .. Our findings demonstrated that the RP4 plasmid carried by the donor strains could be transferred to AOB in the SBR and to Nitrosomonas europaea ATCC 25978.

Conjugation Assay:

Article Title: Horizontal transfer of the multidrug resistance plasmid RP4 inhibits ammonia nitrogen removal dominated by ammonia-oxidizing bacteria.
Article Snippet: .. To achieve this, we established sequencing batch reactors (SBRs) and a conjugation model with E. coli donor strains carrying the RP4 plasmid and a typical ammonia-oxidating (AOB) bacterial strain (Nitrosomonas europaea ATCC 25978) as a recipient to investigate the effect of conjugative transfer of plasmid RP4 on AOB. .. Our findings demonstrated that the RP4 plasmid carried by the donor strains could be transferred to AOB in the SBR and to Nitrosomonas europaea ATCC 25978.

Article Title: Horizontal transfer of the multidrug resistance plasmid RP4 inhibits ammonia nitrogen removal dominated by ammonia-oxidizing bacteria.
Article Snippet: .. Once the RP4 plasmid entered N. europaea ATCC 25978 in the conjugation model, ammonia removal was significantly inhibited and nitrite generation was decreased. ..

Clone Assay:

Image Search Results

Organization of the RP4 plasmid and structural analysis of the PRR1 virion. ( A ) Organization of the major operons in the RP4 plasmid. Tra1 and Tra2 contain the genes for the relaxosome and T4SS, respectively. The Ctl operon helps regulate gene expression, and the Rep operon functions in plasmid replication through initiation at the oriV site. The Par operon encodes the toxin–antitoxin host–defense system ParDE. Lastly, the three antibiotic resistance genes are encoded on bla (β-lactamase enzyme that breaks down ampicillin), aphA (aminoglycoside-3-phosphotransferase enzyme inactivating kanamycin), and the Tet operon (encodes tetA , which produces the tetracycline efflux pump). ( B ) The genes on the Tra1 (transfer 1) operon are shown. Genes in gray are not critical for formation of the T4SS machinery and pilus biogenesis. The origin of transfer (oriT) is highlighted in black. ( C ) The genes on the transfer 2 (Tra2) operon are shown. Genes in gray are not critical for formation of the T4SS machinery or pilus biogenesis. ( D ) Cryo-EM reconstruction of the mature PRR1 virion, showing the Coat (tan), Mat (blue), and the viral RNA (vRNA, gray) with the 3′ end of the vRNA labeled (orange). The virion diameter (292 Å) and Mat prominence (35 Å) are labeled. One stem of the 3′ vRNA extends 20 Å outside the capsid. (Left) Top-down view of the intact virion from the Mat. (Right) Cross-sectional view (rotated 90°), half of the Coat shell is removed to show the 3′ vRNA as well as the rest of the vRNA. ( E ) Secondary structure topology of the Mat PRR1 , highlighting its two major components: the α-helical region (α-region) and β-sheet region (β-region). Two important β-sheet subregions, β4-α1 loop and the tip region, are denoted by arrows. ( F ) The cryo-EM map of the “Mat-less” PRR1 with the Coat shown in pink and the vRNA shown in gray. The lack of Mat density is shown in the inset (viewing angle indicated by the eye cartoon). This class was composed of 67,975 particles (29%) from the PRR1 data set. ( G ) The Coats (tan) immediately surrounding the Mat PRR1 (blue), with the surface contacts between the two labeled red. The surface area of the contacts (803 Å 2 ) is reported below. ( H ) The Coats (maroon) immediately surrounding the Mat (gray) of MS2 (PDB ID: 5TC1) , with the surface contacts between the two labeled red. The surface area of the contacts (1,689 Å 2 ) is reported below.

Journal: Journal of Virology

Article Title: The cryo-EM structure of bacteriophage PRR1 and its role in conjugation inhibition

doi: 10.1128/jvi.00515-26

Figure Lengend Snippet: Organization of the RP4 plasmid and structural analysis of the PRR1 virion. ( A ) Organization of the major operons in the RP4 plasmid. Tra1 and Tra2 contain the genes for the relaxosome and T4SS, respectively. The Ctl operon helps regulate gene expression, and the Rep operon functions in plasmid replication through initiation at the oriV site. The Par operon encodes the toxin–antitoxin host–defense system ParDE. Lastly, the three antibiotic resistance genes are encoded on bla (β-lactamase enzyme that breaks down ampicillin), aphA (aminoglycoside-3-phosphotransferase enzyme inactivating kanamycin), and the Tet operon (encodes tetA , which produces the tetracycline efflux pump). ( B ) The genes on the Tra1 (transfer 1) operon are shown. Genes in gray are not critical for formation of the T4SS machinery and pilus biogenesis. The origin of transfer (oriT) is highlighted in black. ( C ) The genes on the transfer 2 (Tra2) operon are shown. Genes in gray are not critical for formation of the T4SS machinery or pilus biogenesis. ( D ) Cryo-EM reconstruction of the mature PRR1 virion, showing the Coat (tan), Mat (blue), and the viral RNA (vRNA, gray) with the 3′ end of the vRNA labeled (orange). The virion diameter (292 Å) and Mat prominence (35 Å) are labeled. One stem of the 3′ vRNA extends 20 Å outside the capsid. (Left) Top-down view of the intact virion from the Mat. (Right) Cross-sectional view (rotated 90°), half of the Coat shell is removed to show the 3′ vRNA as well as the rest of the vRNA. ( E ) Secondary structure topology of the Mat PRR1 , highlighting its two major components: the α-helical region (α-region) and β-sheet region (β-region). Two important β-sheet subregions, β4-α1 loop and the tip region, are denoted by arrows. ( F ) The cryo-EM map of the “Mat-less” PRR1 with the Coat shown in pink and the vRNA shown in gray. The lack of Mat density is shown in the inset (viewing angle indicated by the eye cartoon). This class was composed of 67,975 particles (29%) from the PRR1 data set. ( G ) The Coats (tan) immediately surrounding the Mat PRR1 (blue), with the surface contacts between the two labeled red. The surface area of the contacts (803 Å 2 ) is reported below. ( H ) The Coats (maroon) immediately surrounding the Mat (gray) of MS2 (PDB ID: 5TC1) , with the surface contacts between the two labeled red. The surface area of the contacts (1,689 Å 2 ) is reported below.

Article Snippet: The RP4 plasmid and bacterial genome extracted were sequenced by Plasmidsaurus.

Techniques: Plasmid Preparation, Gene Expression, Cryo-EM Sample Prep, Labeling

Structural and functional analysis of PRR1 attachment to the RP4 (IncP) pilus. ( A ) Model of a single TrbC pilin monomer with surface-exposed residues that possibly interact with Mat PRR1 shown in stick representations. ( B ) The change in phage infectivity (titer) of each TrbC mutant is shown as the efficiency of plaquing (EOP). Each bar in the infectivity assay represents the mean ± SD of n = 3 biological replicates. The lack of a bar indicates a lack of infection (e.g., S72A). ( C ) The percent change in conjugation efficiencies of TrbC variants carrying mutations in binding residues. Each bar in the conjugation assay represents the mean ± SD of n = 4 biological replicates. The dashed red line represents a transfer efficiency of zero. ( D ) The surface representation of the PRR1 virion (tan and blue) bound to the RP4 pilus (gray), using the Mat of the highest-scored docking model of the RP4–Mat complex as an anchor. The axis of the RP4 pilus is shown as a black line with another black line perpendicular to it. A twofold axis of PRR1 is shown as a red dashed line. The measured tilt angle of binding (between the lines) is 5.6°. ( E ) Side view of the Mat PRR1 footprint (blue) on the RP4 pilus (gray). Two Mat regions participate in pilus binding; the β4-α1 loop is bound to two TrbC pilin monomers (orchid and orange), and the tip region engages one pilin monomer (light pink). The rest of the pilin monomers (gray) are shown in surface representations. The β-region of Mat PRR1 spans three turns on the pilus. The inset shows a 90° rotation of the full Mat bound to the RP4 pilus. ( F ) The tip region (blue shading) from panel E is zoomed in here to show the detailed interactions between the pilus (light pink) and the tip region of the Mat (blue). The gray bond indicates a π-stacking interaction, while the blue line indicates a hydrogen bond. ( G ) The β4-α1 loop (blue shading) from panel E is zoomed in here to show the detailed interactions between the pilus (orchid and orange) and the β4-α1 loop of the Mat (blue).

Journal: Journal of Virology

Article Title: The cryo-EM structure of bacteriophage PRR1 and its role in conjugation inhibition

doi: 10.1128/jvi.00515-26

Figure Lengend Snippet: Structural and functional analysis of PRR1 attachment to the RP4 (IncP) pilus. ( A ) Model of a single TrbC pilin monomer with surface-exposed residues that possibly interact with Mat PRR1 shown in stick representations. ( B ) The change in phage infectivity (titer) of each TrbC mutant is shown as the efficiency of plaquing (EOP). Each bar in the infectivity assay represents the mean ± SD of n = 3 biological replicates. The lack of a bar indicates a lack of infection (e.g., S72A). ( C ) The percent change in conjugation efficiencies of TrbC variants carrying mutations in binding residues. Each bar in the conjugation assay represents the mean ± SD of n = 4 biological replicates. The dashed red line represents a transfer efficiency of zero. ( D ) The surface representation of the PRR1 virion (tan and blue) bound to the RP4 pilus (gray), using the Mat of the highest-scored docking model of the RP4–Mat complex as an anchor. The axis of the RP4 pilus is shown as a black line with another black line perpendicular to it. A twofold axis of PRR1 is shown as a red dashed line. The measured tilt angle of binding (between the lines) is 5.6°. ( E ) Side view of the Mat PRR1 footprint (blue) on the RP4 pilus (gray). Two Mat regions participate in pilus binding; the β4-α1 loop is bound to two TrbC pilin monomers (orchid and orange), and the tip region engages one pilin monomer (light pink). The rest of the pilin monomers (gray) are shown in surface representations. The β-region of Mat PRR1 spans three turns on the pilus. The inset shows a 90° rotation of the full Mat bound to the RP4 pilus. ( F ) The tip region (blue shading) from panel E is zoomed in here to show the detailed interactions between the pilus (light pink) and the tip region of the Mat (blue). The gray bond indicates a π-stacking interaction, while the blue line indicates a hydrogen bond. ( G ) The β4-α1 loop (blue shading) from panel E is zoomed in here to show the detailed interactions between the pilus (orchid and orange) and the β4-α1 loop of the Mat (blue).

Article Snippet: The RP4 plasmid and bacterial genome extracted were sequenced by Plasmidsaurus.

Techniques: Functional Assay, Infection, Mutagenesis, Conjugation Assay, Binding Assay

PRR1 reduces conjugation, and phage/antibiotic selective pressures force mutations in RP4 core genes. ( A ) The effect of PRR1 (red), UV-PRR1 (blue), PP7 (green), and buffer (gray) on RP4 conjugation in P. aeruginosa PAO1Δ pilA (RP4). Each point represents the average of n ≥ 4 replicates. ( B ) A model of the RP4 T4SS. The arrangement of the core proteins within the transfer complex is shown. The protein names are colored to indicate that they contain one of the nine mutations. Those left black do not contain a mutation. This structural model of the RP4 system is derived from its homology to the R388 system (PDB: 7OIU, 7O43, 8RT4, 8RT6, 8RT9, and 8RTD) . ( C ) An image of the spot titer for each RP4 mutant generated from the dual selection assay after being transformed into a new host (see Materials and Methods). Each mutant lacks PRR1 plaques, demonstrating their resistance. ( D ) The conjugation ability of the nine PRR1-resistant mutants. Data represent mean ± SD of n ≥ 8 independent replicates. Statistical significance was determined by one-way ANOVA with Dunnett’s multiple comparison test; all comparisons shown were highly significant. The symbol **** corresponds to a P -value less than 0.0001. ( E ) Conjugation efficiencies of the four transfer-positive mutants in the absence (left) or presence (right) of PRR1 (MOI = 10). Data represent mean ± SD of n = 4 biological replicates. Statistical significance was determined using an unpaired two-tailed t -test for each mutant. P values are traF 1 = 0.0003, trbE 1 < 0.0001, trbH 1 < 0.0001, and trbJ 2 = 0.0002. The symbol **** corresponds to a P -value less than 0.0001 and *** corresponds to a P -value less than 0.001.

Journal: Journal of Virology

Article Title: The cryo-EM structure of bacteriophage PRR1 and its role in conjugation inhibition

doi: 10.1128/jvi.00515-26

Figure Lengend Snippet: PRR1 reduces conjugation, and phage/antibiotic selective pressures force mutations in RP4 core genes. ( A ) The effect of PRR1 (red), UV-PRR1 (blue), PP7 (green), and buffer (gray) on RP4 conjugation in P. aeruginosa PAO1Δ pilA (RP4). Each point represents the average of n ≥ 4 replicates. ( B ) A model of the RP4 T4SS. The arrangement of the core proteins within the transfer complex is shown. The protein names are colored to indicate that they contain one of the nine mutations. Those left black do not contain a mutation. This structural model of the RP4 system is derived from its homology to the R388 system (PDB: 7OIU, 7O43, 8RT4, 8RT6, 8RT9, and 8RTD) . ( C ) An image of the spot titer for each RP4 mutant generated from the dual selection assay after being transformed into a new host (see Materials and Methods). Each mutant lacks PRR1 plaques, demonstrating their resistance. ( D ) The conjugation ability of the nine PRR1-resistant mutants. Data represent mean ± SD of n ≥ 8 independent replicates. Statistical significance was determined by one-way ANOVA with Dunnett’s multiple comparison test; all comparisons shown were highly significant. The symbol **** corresponds to a P -value less than 0.0001. ( E ) Conjugation efficiencies of the four transfer-positive mutants in the absence (left) or presence (right) of PRR1 (MOI = 10). Data represent mean ± SD of n = 4 biological replicates. Statistical significance was determined using an unpaired two-tailed t -test for each mutant. P values are traF 1 = 0.0003, trbE 1 < 0.0001, trbH 1 < 0.0001, and trbJ 2 = 0.0002. The symbol **** corresponds to a P -value less than 0.0001 and *** corresponds to a P -value less than 0.001.

Article Snippet: The RP4 plasmid and bacterial genome extracted were sequenced by Plasmidsaurus.

Techniques: Conjugation Assay, Mutagenesis, Derivative Assay, Generated, Selection, Transformation Assay, Comparison, Two Tailed Test

List of bacterial strains used in this study.

Journal: Scientific Reports

Article Title: Cobalt complexes modulate plasmid conjugation in Escherichia coli and Klebsiella pneumoniae

doi: 10.1038/s41598-024-58895-x

Figure Lengend Snippet: List of bacterial strains used in this study.

Article Snippet: Escherichia coli , Escherichia coli J53 carrying the conjugative RP4 plasmid, which confers resistance to β-lactams, kanamycin, and tetracycline , DSMZ GmbH.

Techniques: Plasmid Preparation

Journal: Scientific Reports

Article Title: Cobalt complexes modulate plasmid conjugation in Escherichia coli and Klebsiella pneumoniae

doi: 10.1038/s41598-024-58895-x

Figure Lengend Snippet: List of plasmids used in this study.

Article Snippet: Escherichia coli , Escherichia coli J53 carrying the conjugative RP4 plasmid, which confers resistance to β-lactams, kanamycin, and tetracycline , DSMZ GmbH.

Techniques: Plasmid Preparation, Derivative Assay, Isolation, Homologous Recombination, Expressing, Selection

The effect of cobalt complexes on the conjugation frequencies of plasmids with different incompatibility groups in liquid LB broth and on LB agar. Conjugation frequencies of ( a ) the IncP plasmid RP4, ( b ) the IncX2 plasmid R6K, ( c ) the IncW R388, and ( d ) the IncN plasmid pKM101, from E. coli J53 to hygromycin resistant E. coli J53 att Tn 7 :: hph in the presence of 100 µg/mL DMSO vehicle control or 100 µg/mL cobalt compound after four-hour incubation. Data shown are the mean ± standard deviation of three independent experiments, each carried out with four biological replicates. Cobalt complexes that significantly affected conjugation frequency compared to DMSO control are indicated with * ( p ≤ 0.05), ** ( p ≤ 0.01) or *** ( p ≤ 0.001). ns, not significant.

Journal: Scientific Reports

Article Title: Cobalt complexes modulate plasmid conjugation in Escherichia coli and Klebsiella pneumoniae

doi: 10.1038/s41598-024-58895-x

Figure Lengend Snippet: The effect of cobalt complexes on the conjugation frequencies of plasmids with different incompatibility groups in liquid LB broth and on LB agar. Conjugation frequencies of ( a ) the IncP plasmid RP4, ( b ) the IncX2 plasmid R6K, ( c ) the IncW R388, and ( d ) the IncN plasmid pKM101, from E. coli J53 to hygromycin resistant E. coli J53 att Tn 7 :: hph in the presence of 100 µg/mL DMSO vehicle control or 100 µg/mL cobalt compound after four-hour incubation. Data shown are the mean ± standard deviation of three independent experiments, each carried out with four biological replicates. Cobalt complexes that significantly affected conjugation frequency compared to DMSO control are indicated with * ( p ≤ 0.05), ** ( p ≤ 0.01) or *** ( p ≤ 0.001). ns, not significant.

Article Snippet: Escherichia coli , Escherichia coli J53 carrying the conjugative RP4 plasmid, which confers resistance to β-lactams, kanamycin, and tetracycline , DSMZ GmbH.

Techniques: Conjugation Assay, Plasmid Preparation, Control, Incubation, Standard Deviation

Conjugation frequency data for RP4, R6K, R388 and pKM101 plasmids in liquid broth and solid agar mating in the presence of 100 µg/mL cobalt compounds or DMSO vehicle control.

Journal: Scientific Reports

Article Title: Cobalt complexes modulate plasmid conjugation in Escherichia coli and Klebsiella pneumoniae

doi: 10.1038/s41598-024-58895-x

Figure Lengend Snippet: Conjugation frequency data for RP4, R6K, R388 and pKM101 plasmids in liquid broth and solid agar mating in the presence of 100 µg/mL cobalt compounds or DMSO vehicle control.

Article Snippet: Escherichia coli , Escherichia coli J53 carrying the conjugative RP4 plasmid, which confers resistance to β-lactams, kanamycin, and tetracycline , DSMZ GmbH.

Techniques: Conjugation Assay, Control

The effect of cobalt complexes on plasmid persistence. The persistence of ( a ) the IncP plasmid RP4, ( b ) the IncX2 plasmid R6K, ( c ) the IncW R388, ( d ) the IncN plasmid pKM101, ( e ) the IncK plasmid pCT with tagged with a gfp gene, and ( f ) the IncFII plasmid pKpQIL tagged with a gfp gene, in the presence of 100 µg/mL of cobalt complexes after 24 and 48 h compared to 100 µg/mL DMSO control. The data shown are the mean ± standard deviation from three independent experiments, each conducted with four biological replicates. ns, not significant.

Journal: Scientific Reports

Article Title: Cobalt complexes modulate plasmid conjugation in Escherichia coli and Klebsiella pneumoniae

doi: 10.1038/s41598-024-58895-x

Figure Lengend Snippet: The effect of cobalt complexes on plasmid persistence. The persistence of ( a ) the IncP plasmid RP4, ( b ) the IncX2 plasmid R6K, ( c ) the IncW R388, ( d ) the IncN plasmid pKM101, ( e ) the IncK plasmid pCT with tagged with a gfp gene, and ( f ) the IncFII plasmid pKpQIL tagged with a gfp gene, in the presence of 100 µg/mL of cobalt complexes after 24 and 48 h compared to 100 µg/mL DMSO control. The data shown are the mean ± standard deviation from three independent experiments, each conducted with four biological replicates. ns, not significant.

Article Snippet: Escherichia coli , Escherichia coli J53 carrying the conjugative RP4 plasmid, which confers resistance to β-lactams, kanamycin, and tetracycline , DSMZ GmbH.

Techniques: Plasmid Preparation, Control, Standard Deviation

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