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Crystallization and preliminary X-ray diffraction studies on the catalytic domain of the chick retinal neurite-inhibitory factor CRYP-2

Girish, TS and Gopal, B (2005) Crystallization and preliminary X-ray diffraction studies on the catalytic domain of the chick retinal neurite-inhibitory factor CRYP-2. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61 (4). pp. 381-383.

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Abstract

The receptor protein tyrosine phosphatase CRYP-2 has been shown to be an inhibitory factor for the growth of retinal axons in the chick. The extra cellular receptor domain of CRYP-2 contains eight fibronectin repeats and studies using the extra cellular domain alone demonstrated the chemorepulsive effect on retinal neurons. The precise role of the intracellular catalytic domain and the mechanism by which its activity is regulated is not known. Determination of the structure of the catalytic domain of CRYP-2 was proposed in an effort to understand the downstream signal transduction mechanism in this system. The cloning, expression, purification and crystallization of the catalytic domain of CRYP-2 are now reported. Preliminary crystallo graphic studies were performed on the diamond-shaped crystals, which grew under oil using the microbatch method at 298 K. Native X-ray diffraction data were collected to 2.9 Angstrom resolution on a home source. The crystals belong to the trigonal space group P3121, with unit-cell parameters a = b = 68.26, c = 244.95 Angstrom. Assuming the presence of two molecules per asymmetric unit, the $V_{M}$ value was 2.7 $A^{3} Da^{-1}$ and the solvent content was 54.8%.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to Blackwell Publishing.
Keywords: receptor protein tyrosine phosphatases;CRYP-2
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 10 Nov 2005
Last Modified: 27 Aug 2008 11:32
URI: http://eprints.iisc.ernet.in/id/eprint/3975

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