Crystallization and preliminary X-ray studies of a recombinant calcium-binding protein from Entamoeba histolytica

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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Abstract

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
Publication:	Acta Crystallographic Section D
Publisher:	International Union of Crystallography
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
URI:	http://eprints.iisc.ac.in/id/eprint/18346

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