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  • Title: Purification, crystallization and preliminary X-ray crystallographic studies on acetolactate decarboxylase.
    Author: Najmudin S, Andersen JT, Patkar SA, Borchert TV, Crout DH, Fülöp V.
    Journal: Acta Crystallogr D Biol Crystallogr; 2003 Jun; 59(Pt 6):1073-5. PubMed ID: 12777778.
    Abstract:
    Acetolactate decarboxylase has the unique ability to decarboxylate both enantiomers of acetolactate to give a single enantiomer of the decarboxylation product, (R)-acetoin. A gene coding for alpha-acetolactate decarboxylase from Bacillus brevis (ATCC 11031) was cloned and overexpressed in B. subtilis. The enzyme was purified in two steps to homogeneity prior to crystallization. Three different diffraction-quality crystal forms were obtained by the hanging-drop vapour-diffusion method using a number of screening conditions. The best crystal form is suitable for structural studies and was grown from solutions containing 20% PEG 2000 MME, 10 mM cadmium chloride and 0.1 M Tris-HCl pH 7.0. They grew to a maximum dimension of approximately 0.4 mm and belong to the trigonal space group P3(1,2)21, with unit-cell parameters a = 47.0, c = 198.9 A. A complete data set was collected to 2 A from a single native crystal using synchrotron radiation.
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