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

Rajaram, V. ; Rajaganapathi, J. ; Khan, F. ; Savithri, H. S. ; Murthy, M. R. N. (2003) Crystallization and preliminary X-ray diffraction studies on recombinant diaminopropionate ammonia lyase from Escherichia coli Acta Crystallographica Section D, 59 . pp. 1668-1669. ISSN 0907-4449

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Official URL: http://scripts.iucr.org/cgi-bin/paper?za5009

Related URL: http://dx.doi.org/10.1107/S0907444903015476

Abstract

Diaminopropionate (DAP) ammonia lyase (a PLP-dependent enzyme; EC 4.3.1.15) catalyzes the α,β-elimination reaction of both L- and D-α,β-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 P41212 (or P43212), with unit-cell parameters a=b=86.01, c=209.56Å, and the other to the monoclinic space group P21, with unit-cell parameters a=87.78, b=94.35, c=96.02Å, β=09.73°. The tetragonal crystals diffracted X-rays to 3.0Å resolution, while diffraction from the monoclinic form extended to 2.5Å. Complete X-ray diffraction data sets have been collected for both crystal forms.

Item Type:Article
Source:Copyright of this article belongs to International Union of Crystallography.
Keywords:DAP Ammonia Lyase; PLP-dependent Enzymes
ID Code:38237
Deposited On:28 Apr 2011 05:57
Last Modified:16 Nov 2011 13:36

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