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- W2166861844 abstract "An extracellular α-type carbonic anhydrase (dCAII) from the salt-tolerant alga Dunaliella salina differs from its mesophilic counterparts in remaining active from zero to multimolar salt concentrations. To gain insight into the outstanding salt tolerance of dCAII, the enzyme was functionally overexpressed in Escherichia coli, purified by affinity chromatography and crystallized by the hanging-drop method. The crystals belonged to space group P21, with unit-cell parameters a = 47.0, b = 119.9, c = 58.5 Å, β = 94.2°. Data from a single crystal were collected to 2.4 Å resolution under cryogenic conditions (120 K) using an R-AXIS IV++ detector mounted on a Rigaku RU-H3R rotating-anode generator. The asymmetric unit contains two molecules of the protein, which corresponds to VM = 2.65 Å3 Da−1 and a solvent content of 52.7%." @default.
- W2166861844 created "2016-06-24" @default.
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- W2166861844 date "2003-05-23" @default.
- W2166861844 modified "2023-09-24" @default.
- W2166861844 title "Identification, cDNA cloning, expression, crystallization and preliminary X-ray analysis of an exceptionally halotolerant carbonic anhydrase from<i>Dunaliella salina</i>" @default.
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- W2166861844 doi "https://doi.org/10.1107/s0907444903007066" @default.
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