Purification, crystallization and preliminary X-ray crystallographic studies on acetolactate decarboxylase
UNSPECIFIED. (2003) Purification, crystallization and preliminary X-ray crystallographic studies on acetolactate decarboxylase. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 59 (Part 6). pp. 1073-1075. ISSN 0907-4449Full text not available from this repository.
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 a-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-HCI 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 Angstrom. A complete data set was collected to 2 Angstrom from a single native crystal using synchrotron radiation.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY|
|Official Date:||June 2003|
|Number of Pages:||3|
|Page Range:||pp. 1073-1075|
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