Crystallization and preliminary X-ray diffraction studies on recombinant diaminopropionate ammonia lyase from Escherichia coli

Rajaram, Venkatesan and Rajaganapathi, Jagannathan and Khan, Farida and Savithri, Handanahal S and Murthy, Mathur RN (2003) Crystallization and preliminary X-ray diffraction studies on recombinant diaminopropionate ammonia lyase from Escherichia coli. In: Acta Crystallographica Section D: Biological Crystallography, 59 (Part 9). pp. 1668-1669.

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Abstract

Diaminopropionate (DAP) ammonia lyase (a PLP-dependent enzyme; EC 4.3.1.15) catalyzes the \alpha,\beta-elimination reaction of both L- and D-\alpha,\beta-diaminopropionate to form pyruvate and ammonia. Escherichia coli DAP ammonia lyase gene was cloned and overexpressed in E. coli and the protein was purified to homogeneity and crystallized using the hanging-drop vapour-diffusion technique. Crystals of two different morphologies were obtained, one of which belonged to the tetragonal space group $P4_12_12$ (or $P4_32_12$), with unit-cell parameters a = b = 86.01, c = 209.56 \AA, and the other to the monoclinic space group $P_21$, with unit-cell parameters a = 87.78, b = 94.35, c = 96.02 \AA, = 109.73°. The tetragonal crystals diffracted X-rays to 3.0 \AA resolution, while diffraction from the monoclinic form extended to 2.5 \AA. Complete X-ray diffraction data sets have been collected for both crystal forms.

Item Type:	Journal Article
Publication:	Acta Crystallographica Section D: Biological Crystallography
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 Division of Biological Sciences > Biochemistry
Date Deposited:	31 May 2006
Last Modified:	19 Sep 2010 04:28
URI:	http://eprints.iisc.ac.in/id/eprint/7211

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