Gopal, B and Suma, R and Murthy, MRN and Bhattacharya, A and Bhattacharya, S (1998) Crystallization and preliminary X-ray studies of a recombinant calcium-binding protein from Entamoeba histolytica. In: Acta Crystallographic Section D, 54 (Part 6). pp. 1442-1445.
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A calcium-binding protein (CaBP) of Entamoeba histolytica was purified from an E. coil recombinant clone carrying the CaBP gene in a pET-3c expression vector using anion exchange and size-exclusion chromatography. Examination of the amino-acid sequence of the recombinant protein suggested that it has four independent EF-hand motifs. The protein dissolved in cacodylate buffer was crystallized using the hanging-drop method with 2-methylpentane-2,4-diol (MPD) as the precipitant. X-ray diffraction data have been collected on these crystals using a MAR Research imaging-plate detector system attached to a Rigaku RU200 rotating-anode X-ray generator. The crystals belong to the hexagonal space group P6(1)22 with unit-cell dimensions of a = b = 96.21, c = 65.48 Angstrom. Preliminary molecular replacement computations suggest that the structure of this protein is likely to be similar to that of calmodulin (CAM).
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to International Union of Crystallography.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||16 Mar 2009 16:59|
|Last Modified:||19 Sep 2010 05:01|
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