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Literature summary for 3.2.1.14 extracted from

  • Okazaki, N.; Arimori, T.; Nakazawa, M.; Miyatake, K.; Ueda, M.; Tamada, T.
    Crystallization and preliminary X-ray diffraction studies of the catalytic domain of a novel chitinase, a member of GH family 23, from the moderately thermophilic bacterium Ralstonia sp. A-471 (2011), Acta Crystallogr. Sect. F, 67, 494-497.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminally His6-tagged mature Ra-ChiC and of Ra-ChiC89–252 domain in Escherichia coli as a soluble proteins Ralstonia sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
purified isolated interdomain loop Ra-ChiC89-252, hanging drop vapour diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution at 20°C, equilibration against reservoir solution, X-ray diffraction structure determination and analysis at 1.85-1.90 A resolution, presence of three, four or five Ra-ChiC89-252 molecules in the asymmetric unit, respectively Ralstonia sp.

Organism

Organism UniProt Comment Textmining
Ralstonia sp.
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-
-
Ralstonia sp. A-471
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant soluble N-terminally His6-tagged mature Ra-ChiC and Ra-ChiC89–252 from Escherichia coli by metal affinity and cation exchange chromatography Ralstonia sp.

Synonyms

Synonyms Comment Organism
ChiC
-
Ralstonia sp.