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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.

SUBMITTER: Cao YL

PROVIDER: S-EPMC3107142 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans.

Cao Yan-Li YL Li Gui-Lan GL Wang Kai-Tuo KT Zhang Hong-Yin HY Li Lan-Fen LF

Acta crystallographica. Section F, Structural biology and crystallization communications 20110525 Pt 6

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 w ...[more]

PMID: 21636911

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