Identification, cDNA cloning, expression, crystallization and preliminary X-ray analysis of an exceptionally halotolerant carbonic anhydrase from Dunaliella salina

Lakshmanane, Prem, Greenblatt, Harry M., Bageshwar, Umesh K., Savchenko, Umesh K., Gokhman, Irena, Zamir, Ada and Sussman, Joel L. (2003) Identification, cDNA cloning, expression, crystallization and preliminary X-ray analysis of an exceptionally halotolerant carbonic anhydrase from Dunaliella salina. Acta Crystallographica Section D: Biological Crystallography, 59 6: 1084-1086. doi:10.1107/S0907444903007066

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Author Lakshmanane, Prem
Greenblatt, Harry M.
Bageshwar, Umesh K.
Savchenko, Umesh K.
Gokhman, Irena
Zamir, Ada
Sussman, Joel L.
Title Identification, cDNA cloning, expression, crystallization and preliminary X-ray analysis of an exceptionally halotolerant carbonic anhydrase from Dunaliella salina
Journal name Acta Crystallographica Section D: Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
1399-0047
Publication date 2003-06-01
Sub-type Article (original research)
DOI 10.1107/S0907444903007066
Open Access Status File (Publisher version)
Volume 59
Issue 6
Start page 1084
End page 1086
Total pages 3
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell Publishing
Language eng
Formatted 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%.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Created: Tue, 06 Sep 2011, 11:06:54 EST by Susan Allen on behalf of Institute for Molecular Bioscience