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bacillus halodurans atcc baa 125  (ATCC)


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    Structured Review

    ATCC bacillus halodurans atcc baa 125
    Comparison of the enzyme properties of various L-RhIs
    Bacillus Halodurans Atcc Baa 125, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 122 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "L-rhamnose isomerase: a crucial enzyme for rhamnose catabolism and conversion of rare sugars"

    Article Title: L-rhamnose isomerase: a crucial enzyme for rhamnose catabolism and conversion of rare sugars

    Journal: Applied Microbiology and Biotechnology

    doi: 10.1007/s00253-024-13325-w

    Comparison of the enzyme properties of various L-RhIs
    Figure Legend Snippet: Comparison of the enzyme properties of various L-RhIs

    Techniques Used: Comparison, Sequencing



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    93
    ATCC bacillus halodurans atcc baa 125
    Comparison of the enzyme properties of various L-RhIs
    Bacillus Halodurans Atcc Baa 125, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    DSMZ halalkalibacterium halodurans
    A. Schematic overview of the pipeline for identifying bacteria targeted by peptidoglycan hydrolases. The cell wall/peptidoglycan binding domain of a putative archaeal peptidoglycan hydrolase (PGH) is searched against a database of archaeal and bacterial PGH homologs, using either primary sequence (HMMer) or structural homology (Foldseek) searches. Domain matches are ranked by similarity, normalized to the score obtained by matching against the query protein itself. B. The cell wall binding domains of phage endolysins are typically most similar to the cell wall binding domains of their (predicted) bacterial hosts compared to domains from other bacteria. C. Probability that, for a given archaeal query protein, bacteria from the same biome are identified amongst the top 10 hits. Biome labels were applied as described in and results are aggregated at the biome level; the size of each circle indicates the likelihood ratio associated with a given biome. D. Ranking of homologous bacterial hits against the PG binding 1 domain of Woldo based on sequence vs. structural homology scores (Spearman’s rho = 0.48). E. Enrichment of bacterial phyla amongst top 10 predicted targets across PGH homologs. See for how enrichment was computed F. Results of spotting various supernatants onto lawns of <t>Halalkalibacterium</t> <t>halodurans</t> , Phycicoccus endophyticus , and Virgibacillus salexigens . a,b: top fraction (>3 kDa) of supernatant from Haloferax volcanii expressing an intact (a) or catalytic mutant (b) version of Woldo; c,d: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing an intact (c) or catalytic mutant (d) version of Woldo; e: unfiltered supernatant from Halogranum salarium B-1; f,g: top fraction (>3 kDa) of supernatant from H. volcanii expressing (f) Danwoldo or (g) and empty plasmid control; h,i: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing (h) Danwoldo or (i) and empty plasmid control. G. Colony forming assays for different bacteria following treatment with supernatant from H. volcanii expressing Woldo, Danwoldo, or the control (bottom fraction of Woldo-expressing H. volcanii H1424 supernatant). Error bars represent standard deviation from three biological replicates. H. Images of bacterial cells following exposure to H. volcanii supernatants expressing Woldo, Danwoldo or the control (as above). Bacteria are stained using LIVE/DEAD BacLight bacterial viability staining kit with ingress of red dye into bacterial cells indicative of cells with terminally compromised cell wall integrity. Code and data are available at zenodo.org/records/15534318 (“notebook/figure3.ipynb” and “data/figure3/”, respectively).
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    ATCC nra 10 bacillus halodurans atcc baa
    A. Schematic overview of the pipeline for identifying bacteria targeted by peptidoglycan hydrolases. The cell wall/peptidoglycan binding domain of a putative archaeal peptidoglycan hydrolase (PGH) is searched against a database of archaeal and bacterial PGH homologs, using either primary sequence (HMMer) or structural homology (Foldseek) searches. Domain matches are ranked by similarity, normalized to the score obtained by matching against the query protein itself. B. The cell wall binding domains of phage endolysins are typically most similar to the cell wall binding domains of their (predicted) bacterial hosts compared to domains from other bacteria. C. Probability that, for a given archaeal query protein, bacteria from the same biome are identified amongst the top 10 hits. Biome labels were applied as described in and results are aggregated at the biome level; the size of each circle indicates the likelihood ratio associated with a given biome. D. Ranking of homologous bacterial hits against the PG binding 1 domain of Woldo based on sequence vs. structural homology scores (Spearman’s rho = 0.48). E. Enrichment of bacterial phyla amongst top 10 predicted targets across PGH homologs. See for how enrichment was computed F. Results of spotting various supernatants onto lawns of <t>Halalkalibacterium</t> <t>halodurans</t> , Phycicoccus endophyticus , and Virgibacillus salexigens . a,b: top fraction (>3 kDa) of supernatant from Haloferax volcanii expressing an intact (a) or catalytic mutant (b) version of Woldo; c,d: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing an intact (c) or catalytic mutant (d) version of Woldo; e: unfiltered supernatant from Halogranum salarium B-1; f,g: top fraction (>3 kDa) of supernatant from H. volcanii expressing (f) Danwoldo or (g) and empty plasmid control; h,i: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing (h) Danwoldo or (i) and empty plasmid control. G. Colony forming assays for different bacteria following treatment with supernatant from H. volcanii expressing Woldo, Danwoldo, or the control (bottom fraction of Woldo-expressing H. volcanii H1424 supernatant). Error bars represent standard deviation from three biological replicates. H. Images of bacterial cells following exposure to H. volcanii supernatants expressing Woldo, Danwoldo or the control (as above). Bacteria are stained using LIVE/DEAD BacLight bacterial viability staining kit with ingress of red dye into bacterial cells indicative of cells with terminally compromised cell wall integrity. Code and data are available at zenodo.org/records/15534318 (“notebook/figure3.ipynb” and “data/figure3/”, respectively).
    Nra 10 Bacillus Halodurans Atcc Baa, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC bacillus halodurans
    A. Schematic overview of the pipeline for identifying bacteria targeted by peptidoglycan hydrolases. The cell wall/peptidoglycan binding domain of a putative archaeal peptidoglycan hydrolase (PGH) is searched against a database of archaeal and bacterial PGH homologs, using either primary sequence (HMMer) or structural homology (Foldseek) searches. Domain matches are ranked by similarity, normalized to the score obtained by matching against the query protein itself. B. The cell wall binding domains of phage endolysins are typically most similar to the cell wall binding domains of their (predicted) bacterial hosts compared to domains from other bacteria. C. Probability that, for a given archaeal query protein, bacteria from the same biome are identified amongst the top 10 hits. Biome labels were applied as described in and results are aggregated at the biome level; the size of each circle indicates the likelihood ratio associated with a given biome. D. Ranking of homologous bacterial hits against the PG binding 1 domain of Woldo based on sequence vs. structural homology scores (Spearman’s rho = 0.48). E. Enrichment of bacterial phyla amongst top 10 predicted targets across PGH homologs. See for how enrichment was computed F. Results of spotting various supernatants onto lawns of <t>Halalkalibacterium</t> <t>halodurans</t> , Phycicoccus endophyticus , and Virgibacillus salexigens . a,b: top fraction (>3 kDa) of supernatant from Haloferax volcanii expressing an intact (a) or catalytic mutant (b) version of Woldo; c,d: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing an intact (c) or catalytic mutant (d) version of Woldo; e: unfiltered supernatant from Halogranum salarium B-1; f,g: top fraction (>3 kDa) of supernatant from H. volcanii expressing (f) Danwoldo or (g) and empty plasmid control; h,i: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing (h) Danwoldo or (i) and empty plasmid control. G. Colony forming assays for different bacteria following treatment with supernatant from H. volcanii expressing Woldo, Danwoldo, or the control (bottom fraction of Woldo-expressing H. volcanii H1424 supernatant). Error bars represent standard deviation from three biological replicates. H. Images of bacterial cells following exposure to H. volcanii supernatants expressing Woldo, Danwoldo or the control (as above). Bacteria are stained using LIVE/DEAD BacLight bacterial viability staining kit with ingress of red dye into bacterial cells indicative of cells with terminally compromised cell wall integrity. Code and data are available at zenodo.org/records/15534318 (“notebook/figure3.ipynb” and “data/figure3/”, respectively).
    Bacillus Halodurans, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC bacillus sp
    A. Schematic overview of the pipeline for identifying bacteria targeted by peptidoglycan hydrolases. The cell wall/peptidoglycan binding domain of a putative archaeal peptidoglycan hydrolase (PGH) is searched against a database of archaeal and bacterial PGH homologs, using either primary sequence (HMMer) or structural homology (Foldseek) searches. Domain matches are ranked by similarity, normalized to the score obtained by matching against the query protein itself. B. The cell wall binding domains of phage endolysins are typically most similar to the cell wall binding domains of their (predicted) bacterial hosts compared to domains from other bacteria. C. Probability that, for a given archaeal query protein, bacteria from the same biome are identified amongst the top 10 hits. Biome labels were applied as described in and results are aggregated at the biome level; the size of each circle indicates the likelihood ratio associated with a given biome. D. Ranking of homologous bacterial hits against the PG binding 1 domain of Woldo based on sequence vs. structural homology scores (Spearman’s rho = 0.48). E. Enrichment of bacterial phyla amongst top 10 predicted targets across PGH homologs. See for how enrichment was computed F. Results of spotting various supernatants onto lawns of <t>Halalkalibacterium</t> <t>halodurans</t> , Phycicoccus endophyticus , and Virgibacillus salexigens . a,b: top fraction (>3 kDa) of supernatant from Haloferax volcanii expressing an intact (a) or catalytic mutant (b) version of Woldo; c,d: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing an intact (c) or catalytic mutant (d) version of Woldo; e: unfiltered supernatant from Halogranum salarium B-1; f,g: top fraction (>3 kDa) of supernatant from H. volcanii expressing (f) Danwoldo or (g) and empty plasmid control; h,i: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing (h) Danwoldo or (i) and empty plasmid control. G. Colony forming assays for different bacteria following treatment with supernatant from H. volcanii expressing Woldo, Danwoldo, or the control (bottom fraction of Woldo-expressing H. volcanii H1424 supernatant). Error bars represent standard deviation from three biological replicates. H. Images of bacterial cells following exposure to H. volcanii supernatants expressing Woldo, Danwoldo or the control (as above). Bacteria are stained using LIVE/DEAD BacLight bacterial viability staining kit with ingress of red dye into bacterial cells indicative of cells with terminally compromised cell wall integrity. Code and data are available at zenodo.org/records/15534318 (“notebook/figure3.ipynb” and “data/figure3/”, respectively).
    Bacillus Sp, 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
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    Dietmar Hopp Stiftung thermostable alkaline protease from bacillus halodurans se5
    A. Schematic overview of the pipeline for identifying bacteria targeted by peptidoglycan hydrolases. The cell wall/peptidoglycan binding domain of a putative archaeal peptidoglycan hydrolase (PGH) is searched against a database of archaeal and bacterial PGH homologs, using either primary sequence (HMMer) or structural homology (Foldseek) searches. Domain matches are ranked by similarity, normalized to the score obtained by matching against the query protein itself. B. The cell wall binding domains of phage endolysins are typically most similar to the cell wall binding domains of their (predicted) bacterial hosts compared to domains from other bacteria. C. Probability that, for a given archaeal query protein, bacteria from the same biome are identified amongst the top 10 hits. Biome labels were applied as described in and results are aggregated at the biome level; the size of each circle indicates the likelihood ratio associated with a given biome. D. Ranking of homologous bacterial hits against the PG binding 1 domain of Woldo based on sequence vs. structural homology scores (Spearman’s rho = 0.48). E. Enrichment of bacterial phyla amongst top 10 predicted targets across PGH homologs. See for how enrichment was computed F. Results of spotting various supernatants onto lawns of <t>Halalkalibacterium</t> <t>halodurans</t> , Phycicoccus endophyticus , and Virgibacillus salexigens . a,b: top fraction (>3 kDa) of supernatant from Haloferax volcanii expressing an intact (a) or catalytic mutant (b) version of Woldo; c,d: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing an intact (c) or catalytic mutant (d) version of Woldo; e: unfiltered supernatant from Halogranum salarium B-1; f,g: top fraction (>3 kDa) of supernatant from H. volcanii expressing (f) Danwoldo or (g) and empty plasmid control; h,i: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing (h) Danwoldo or (i) and empty plasmid control. G. Colony forming assays for different bacteria following treatment with supernatant from H. volcanii expressing Woldo, Danwoldo, or the control (bottom fraction of Woldo-expressing H. volcanii H1424 supernatant). Error bars represent standard deviation from three biological replicates. H. Images of bacterial cells following exposure to H. volcanii supernatants expressing Woldo, Danwoldo or the control (as above). Bacteria are stained using LIVE/DEAD BacLight bacterial viability staining kit with ingress of red dye into bacterial cells indicative of cells with terminally compromised cell wall integrity. Code and data are available at zenodo.org/records/15534318 (“notebook/figure3.ipynb” and “data/figure3/”, respectively).
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    DSMZ b halodurans
    Microscopic images (ranging in magnification from 24× to 28×) of mortar samples with a crack width of 0.130-0.136 mm before and after 7 and 35 days of healing using microcapsules with different bacterial species: ( a ) B. pseudofirmus ; ( b ) B. cohnii ; ( c ) B. <t>halodurans.</t> Here, w i is the initial crack width; w t is the crack width after healing; H c is the calculated healing ratio. The blue arrows indicate the location where the width of the gap was measured.
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    Image Search Results


    Comparison of the enzyme properties of various L-RhIs

    Journal: Applied Microbiology and Biotechnology

    Article Title: L-rhamnose isomerase: a crucial enzyme for rhamnose catabolism and conversion of rare sugars

    doi: 10.1007/s00253-024-13325-w

    Figure Lengend Snippet: Comparison of the enzyme properties of various L-RhIs

    Article Snippet: Bacillus halodurans ATCC BAA-125 , 121/48, homodimer homotetramer* , Halalkalibacterium halodurans ATCC BAA-125 (BAB05271.1), 418 a.a., 48,178 Da , 7.0 , 70 , Mn 2+ , 528 , 0.28 , 187 , L-lyxose > , L-mannose, D-gulose, L-talose , Prabhu et al. Prabhu et al. * .

    Techniques: Comparison, Sequencing

    A. Schematic overview of the pipeline for identifying bacteria targeted by peptidoglycan hydrolases. The cell wall/peptidoglycan binding domain of a putative archaeal peptidoglycan hydrolase (PGH) is searched against a database of archaeal and bacterial PGH homologs, using either primary sequence (HMMer) or structural homology (Foldseek) searches. Domain matches are ranked by similarity, normalized to the score obtained by matching against the query protein itself. B. The cell wall binding domains of phage endolysins are typically most similar to the cell wall binding domains of their (predicted) bacterial hosts compared to domains from other bacteria. C. Probability that, for a given archaeal query protein, bacteria from the same biome are identified amongst the top 10 hits. Biome labels were applied as described in and results are aggregated at the biome level; the size of each circle indicates the likelihood ratio associated with a given biome. D. Ranking of homologous bacterial hits against the PG binding 1 domain of Woldo based on sequence vs. structural homology scores (Spearman’s rho = 0.48). E. Enrichment of bacterial phyla amongst top 10 predicted targets across PGH homologs. See for how enrichment was computed F. Results of spotting various supernatants onto lawns of Halalkalibacterium halodurans , Phycicoccus endophyticus , and Virgibacillus salexigens . a,b: top fraction (>3 kDa) of supernatant from Haloferax volcanii expressing an intact (a) or catalytic mutant (b) version of Woldo; c,d: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing an intact (c) or catalytic mutant (d) version of Woldo; e: unfiltered supernatant from Halogranum salarium B-1; f,g: top fraction (>3 kDa) of supernatant from H. volcanii expressing (f) Danwoldo or (g) and empty plasmid control; h,i: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing (h) Danwoldo or (i) and empty plasmid control. G. Colony forming assays for different bacteria following treatment with supernatant from H. volcanii expressing Woldo, Danwoldo, or the control (bottom fraction of Woldo-expressing H. volcanii H1424 supernatant). Error bars represent standard deviation from three biological replicates. H. Images of bacterial cells following exposure to H. volcanii supernatants expressing Woldo, Danwoldo or the control (as above). Bacteria are stained using LIVE/DEAD BacLight bacterial viability staining kit with ingress of red dye into bacterial cells indicative of cells with terminally compromised cell wall integrity. Code and data are available at zenodo.org/records/15534318 (“notebook/figure3.ipynb” and “data/figure3/”, respectively).

    Journal: PLOS Biology

    Article Title: Archaea produce peptidoglycan hydrolases that kill bacteria

    doi: 10.1371/journal.pbio.3003235

    Figure Lengend Snippet: A. Schematic overview of the pipeline for identifying bacteria targeted by peptidoglycan hydrolases. The cell wall/peptidoglycan binding domain of a putative archaeal peptidoglycan hydrolase (PGH) is searched against a database of archaeal and bacterial PGH homologs, using either primary sequence (HMMer) or structural homology (Foldseek) searches. Domain matches are ranked by similarity, normalized to the score obtained by matching against the query protein itself. B. The cell wall binding domains of phage endolysins are typically most similar to the cell wall binding domains of their (predicted) bacterial hosts compared to domains from other bacteria. C. Probability that, for a given archaeal query protein, bacteria from the same biome are identified amongst the top 10 hits. Biome labels were applied as described in and results are aggregated at the biome level; the size of each circle indicates the likelihood ratio associated with a given biome. D. Ranking of homologous bacterial hits against the PG binding 1 domain of Woldo based on sequence vs. structural homology scores (Spearman’s rho = 0.48). E. Enrichment of bacterial phyla amongst top 10 predicted targets across PGH homologs. See for how enrichment was computed F. Results of spotting various supernatants onto lawns of Halalkalibacterium halodurans , Phycicoccus endophyticus , and Virgibacillus salexigens . a,b: top fraction (>3 kDa) of supernatant from Haloferax volcanii expressing an intact (a) or catalytic mutant (b) version of Woldo; c,d: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing an intact (c) or catalytic mutant (d) version of Woldo; e: unfiltered supernatant from Halogranum salarium B-1; f,g: top fraction (>3 kDa) of supernatant from H. volcanii expressing (f) Danwoldo or (g) and empty plasmid control; h,i: bottom fraction (<3 kDa) of supernatant from H. volcanii expressing (h) Danwoldo or (i) and empty plasmid control. G. Colony forming assays for different bacteria following treatment with supernatant from H. volcanii expressing Woldo, Danwoldo, or the control (bottom fraction of Woldo-expressing H. volcanii H1424 supernatant). Error bars represent standard deviation from three biological replicates. H. Images of bacterial cells following exposure to H. volcanii supernatants expressing Woldo, Danwoldo or the control (as above). Bacteria are stained using LIVE/DEAD BacLight bacterial viability staining kit with ingress of red dye into bacterial cells indicative of cells with terminally compromised cell wall integrity. Code and data are available at zenodo.org/records/15534318 (“notebook/figure3.ipynb” and “data/figure3/”, respectively).

    Article Snippet: Halogranum salarium B-1 (DSM-23171), Halalkalibacterium halodurans (DSM-18197), Phycicoccus endophyticus (DSM-100020), and Virgibacillus salexigens (DSM-11483) were obtained from the Deutsche Sammlung von Mikroorganismen und Zellkulturen (DSMZ).

    Techniques: Bacteria, Binding Assay, Sequencing, Expressing, Mutagenesis, Plasmid Preparation, Control, Standard Deviation, Staining

    Microscopic images (ranging in magnification from 24× to 28×) of mortar samples with a crack width of 0.130-0.136 mm before and after 7 and 35 days of healing using microcapsules with different bacterial species: ( a ) B. pseudofirmus ; ( b ) B. cohnii ; ( c ) B. halodurans. Here, w i is the initial crack width; w t is the crack width after healing; H c is the calculated healing ratio. The blue arrows indicate the location where the width of the gap was measured.

    Journal: Microorganisms

    Article Title: Bacterial Viability in Self-Healing Concrete: A Case Study of Non-Ureolytic Bacillus Species

    doi: 10.3390/microorganisms11102402

    Figure Lengend Snippet: Microscopic images (ranging in magnification from 24× to 28×) of mortar samples with a crack width of 0.130-0.136 mm before and after 7 and 35 days of healing using microcapsules with different bacterial species: ( a ) B. pseudofirmus ; ( b ) B. cohnii ; ( c ) B. halodurans. Here, w i is the initial crack width; w t is the crack width after healing; H c is the calculated healing ratio. The blue arrows indicate the location where the width of the gap was measured.

    Article Snippet: Three alkaliphilic and spore-forming bacteria species, i.e., B. pseudofirmus (DSM 8715), B. cohnii (DSM 6307), and B. halodurans (DSM 497), were purchased from the German Collection of Microorganisms and Cell Cultures (DSMZ), Braunschweig, Germany.

    Techniques:

    Microscopic images (ranging in magnification from 24× to 28×) of mortar samples with a crack width of 0.213-0.288 mm before and after 14 and 35 days of healing using microcapsules with different bacterial species: ( a ) B. pseudofirmus ; ( b ) B. cohnii ; ( c ) B . halodurans. Here, w i is the initial crack width; w t is the crack width after healing; H c is the calculated healing ratio. The blue arrows indicate the location where the width of the gap was measured.

    Journal: Microorganisms

    Article Title: Bacterial Viability in Self-Healing Concrete: A Case Study of Non-Ureolytic Bacillus Species

    doi: 10.3390/microorganisms11102402

    Figure Lengend Snippet: Microscopic images (ranging in magnification from 24× to 28×) of mortar samples with a crack width of 0.213-0.288 mm before and after 14 and 35 days of healing using microcapsules with different bacterial species: ( a ) B. pseudofirmus ; ( b ) B. cohnii ; ( c ) B . halodurans. Here, w i is the initial crack width; w t is the crack width after healing; H c is the calculated healing ratio. The blue arrows indicate the location where the width of the gap was measured.

    Article Snippet: Three alkaliphilic and spore-forming bacteria species, i.e., B. pseudofirmus (DSM 8715), B. cohnii (DSM 6307), and B. halodurans (DSM 497), were purchased from the German Collection of Microorganisms and Cell Cultures (DSMZ), Braunschweig, Germany.

    Techniques: