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bacteria staphylococcus aureus strain  (ATCC)


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    Structured Review

    ATCC bacteria staphylococcus aureus strain
    Bacteria Staphylococcus Aureus Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 35890 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 35890 article reviews
    bacteria staphylococcus aureus strain - by Bioz Stars, 2026-03
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    ATCC bacteria b paralicheniformis strain atcc 9945a
    Structure properties of the α-amylase AmyBL159 (the model was predicted by AlphaFold 3): ( A , B )—a domain organization in overall structure of the α-amylase AmyBL159; ( C , D )—a superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. paralicheniformis strain ATCC <t>9945a</t> (RCSB PDB acc. no.: <t>6TOZ,</t> carbon atoms are colored in blue) with presentation of the active cleft with catalytic residues (red color); ( E , F )—a superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. paralicheniformis strain ATCC 9945a (RCSB PDB acc. no.: 6TOZ, carbon atoms are colored in blue) with presentation of the Ca-Na-Ca triad; ( G , H )—a superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. licheniformis (RCSB PDB acc. no.: 1OB0, carbon atoms are colored in coral) with presentation of the mutation sites compared to wild type of the α-amylase (RCSB PDB acc. no.: 1BLI), the front view; ( I , J )—the back view of the superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. licheniformis (RCSB PDB acc. no.: 1OB0, carbon atoms are colored in coral) with presentation of the mutation sites compared to wild type of the α-amylase (RCSB PDB acc. no.: 1BLI). The molecule of substrate analogue (acarbose) presented in all structures is colored in blue. Other atoms as well as calcium (green sphere) and sodium (magenta sphere) ions are colored as element type.
    Bacteria B Paralicheniformis Strain Atcc 9945a, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Structure properties of the α-amylase AmyBL159 (the model was predicted by AlphaFold 3): ( A , B )—a domain organization in overall structure of the α-amylase AmyBL159; ( C , D )—a superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. paralicheniformis strain ATCC 9945a (RCSB PDB acc. no.: 6TOZ, carbon atoms are colored in blue) with presentation of the active cleft with catalytic residues (red color); ( E , F )—a superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. paralicheniformis strain ATCC 9945a (RCSB PDB acc. no.: 6TOZ, carbon atoms are colored in blue) with presentation of the Ca-Na-Ca triad; ( G , H )—a superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. licheniformis (RCSB PDB acc. no.: 1OB0, carbon atoms are colored in coral) with presentation of the mutation sites compared to wild type of the α-amylase (RCSB PDB acc. no.: 1BLI), the front view; ( I , J )—the back view of the superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. licheniformis (RCSB PDB acc. no.: 1OB0, carbon atoms are colored in coral) with presentation of the mutation sites compared to wild type of the α-amylase (RCSB PDB acc. no.: 1BLI). The molecule of substrate analogue (acarbose) presented in all structures is colored in blue. Other atoms as well as calcium (green sphere) and sodium (magenta sphere) ions are colored as element type.

    Journal: Microorganisms

    Article Title: Recombinant Forms of α-Amylase AmyBL159 from a Thermophilic Bacterium Bacillus licheniformis MGMM159: The Effect of the Expression System on the Enzyme Properties

    doi: 10.3390/microorganisms13122747

    Figure Lengend Snippet: Structure properties of the α-amylase AmyBL159 (the model was predicted by AlphaFold 3): ( A , B )—a domain organization in overall structure of the α-amylase AmyBL159; ( C , D )—a superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. paralicheniformis strain ATCC 9945a (RCSB PDB acc. no.: 6TOZ, carbon atoms are colored in blue) with presentation of the active cleft with catalytic residues (red color); ( E , F )—a superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. paralicheniformis strain ATCC 9945a (RCSB PDB acc. no.: 6TOZ, carbon atoms are colored in blue) with presentation of the Ca-Na-Ca triad; ( G , H )—a superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. licheniformis (RCSB PDB acc. no.: 1OB0, carbon atoms are colored in coral) with presentation of the mutation sites compared to wild type of the α-amylase (RCSB PDB acc. no.: 1BLI), the front view; ( I , J )—the back view of the superposition of the α-amylase AmyBL159 (carbon atoms are colored in gray) and α-amylase from B. licheniformis (RCSB PDB acc. no.: 1OB0, carbon atoms are colored in coral) with presentation of the mutation sites compared to wild type of the α-amylase (RCSB PDB acc. no.: 1BLI). The molecule of substrate analogue (acarbose) presented in all structures is colored in blue. Other atoms as well as calcium (green sphere) and sodium (magenta sphere) ions are colored as element type.

    Article Snippet: Another enzyme with a known crystal structure similar to the α-amylases AmyBL159 was α-amylase from bacteria B. paralicheniformis strain ATCC 9945a (RCSB PDB acc. no.: 6TOZ; [ ], where 20 amino acid substitutions were found.

    Techniques: Mutagenesis