title: Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans.
abstract: Argininosuccinate lyase (ASL) is an important enzyme in arginine synthesis and the urea cycle, which are highly conserved from bacteria to eukaryotes. The gene encoding Streptococcus mutans ASL (smASL) was amplified and cloned into expression vector pET28a. The recombinant smASL protein was expressed in a soluble form in Escherichia coli strain BL21 (DE3) and purified to homogeneity by two-step column chromatography. Crystals suitable for X-ray analysis were obtained and X-ray diffraction data were collected to a resolution of 2.5 Å. The crystals belonged to space group R3, with unit-cell parameters a = b = 254.5, c = 78.3 Å.
authors.affiliation: Peking University Hospital, Peking University, Beijing, People's Republic of China.
authors.forename: Yan-Li
authors.initials: YL
authors.lastname: Cao
authors.forename: Gui-Lan
authors.initials: GL
authors.lastname: Li
authors.forename: Kai-Tuo
authors.initials: KT
authors.lastname: Wang
authors.forename: Hong-Yin
authors.initials: HY
authors.lastname: Zhang
authors.forename: Lan-Fen
authors.initials: LF
authors.lastname: Li
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001123:Argininosuccinate Lyase / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013295:Streptococcus mutans / Q000201:enzymology*
chemical_list: D001123:Argininosuccinate Lyase