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Literature summary for 3.1.1.58 extracted from

  • Fadouloglou, V.E.; Kapanidou, M.; Agiomirgianaki, A.; Arnaouteli, S.; Bouriotis, V.; Glykos, N.M.; Kokkinidis, M.
    Structure determination through homology modelling and torsion-angle simulated annealing: application to a polysaccharide deacetylase from Bacillus cereus (2013), Acta Crystallogr. Sect. D, 69, 276-283.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain DE3 pLysS Bacillus cereus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, hanging drop vapour diffusion, protein in 50 mM HEPES-NaOH, pH 6.8, 200 mM NaCl is mixed with 25-30% w/v PEG 3350, 100 mM Tris-HCl, pH 7.5-8.0, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement procedure, method overview. Construction of putative models of the C-terminal domain of the protein using a multitude of homology modelling algorithms, and test for the presence of signal in molecular replacement calculations, slow-cooling torsion-angle simulated annealing Bacillus cereus

Organism

Organism UniProt Comment Textmining
Bacillus cereus Q81IM3
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Bacillus cereus ATCC 14579 Q81IM3
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain DE3 pLysS by cation exchange chromatography and gel filtration Bacillus cereus

Synonyms

Synonyms Comment Organism
BC0361
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Bacillus cereus
polysaccharide deacetylase
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Bacillus cereus

General Information

General Information Comment Organism
additional information structure determination and analysis using a molecular replacement procedure, method overview. Contruction of putative models of the C-terminal domain of the protein using a multitude of homology-modelling algorithms, and test for the presence of signal in molecular replacement calculations, slow-cooling torsion-angle simulated annealing Bacillus cereus