The Library
Purification, crystallization and preliminary X-ray crystallographic studies on acetolactate decarboxylase
Tools
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 0907-4449.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
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 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 | ||||
Publisher: | BLACKWELL MUNKSGAARD | ||||
ISSN: | 0907-4449 | ||||
Official Date: | June 2003 | ||||
Dates: |
|
||||
Volume: | 59 | ||||
Number: | Part 6 | ||||
Number of Pages: | 3 | ||||
Page Range: | pp. 1073-1075 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |