title: Preliminary X-ray crystallographic studies of Bacillus subtilis SpeA protein.
abstract: The speA gene in Bacillus subtilis encodes arginine decarboxylase, which catalyzes the conversion of arginine to agmatine. Arginine decarboxylase is an important enzyme in polyamine metabolism in B. subtilis. In order to further illustrate the catalytic mechanism of arginine decarboxylase by determining the three-dimensional structure of the enzyme, the speA gene was amplified from B. subtilis genomic DNA and cloned into the expression vector pET-28a(+). SpeA was expressed in Escherichia coli and purified to homogeneity by nickel-chelation chromatography followed by size-exclusion chromatography. High-quality crystals were obtained using the hanging-drop vapour-diffusion method at 289 K. The best crystal diffracted to 2.0 A resolution and belonged to space group P2(1), with unit-cell parameters a = 86.4, b = 63.3 c = 103.3 A, beta = 113.9 degrees .
authors.affiliation: Peking University, Beijing, People's Republic of China.
authors.forename: Xiao Yan
authors.initials: XY
authors.lastname: Liu
authors.forename: Jian
authors.initials: J
authors.lastname: Lei
authors.forename: Xiang
authors.initials: X
authors.lastname: Liu
authors.forename: Xiao Dong
authors.initials: XD
authors.lastname: Su
authors.forename: Lanfen
authors.initials: L
authors.lastname: Li
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray
chemical_list: D001426:Bacterial Proteins