title: Expression, purification, crystallization and preliminary X-ray analysis of ribitol-5-phosphate cytidylyltransferase from Bacillus subtilis.
abstract: TarI is a ribitol-5-phosphate cytidylyltransferase that catalyzes the formation of CDP-ribitol, which is involved in the biosynthesis of wall teichoic acids, from CTP and ribitol 5-phosphate. TarI from Bacillus subtilis (BsTarI) was purified and crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 1.78 Å and belonged to the monoclinic space group C2, with unit-cell parameters a = 103.74, b = 60.97, c = 91.80 Å, β = 113.48°. The initial structural model indicated that the crystals of BsTarI contained a dimer in the asymmetric unit.
authors.affiliation: Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei City 100, Taiwan.
authors.forename: Sheng-Chia
authors.initials: SC
authors.lastname: Chen
authors.forename: Chia Shin
authors.initials: CS
authors.lastname: Yang
authors.forename: Ching-Ting
authors.initials: CT
authors.lastname: Lin
authors.forename: Nei-Li
authors.initials: NL
authors.lastname: Chan
authors.forename: Ming-Chung
authors.initials: MC
authors.lastname: Chang
authors.forename: Yeh
authors.initials: Y
authors.lastname: Chen
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D008958:Models, Molecular; D009713:Nucleotidyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D017434:Protein Structure, Tertiary
chemical_list: D009713:Nucleotidyltransferases; C032634:D-ribitol-5-phosphate cytidylyltransferase