Open AccessCrystallization and preliminary X‐ray analysis of argininosuccinate lyase from Streptococcus mutans
Author(s) -
Cao YanLi,
Li GuiLan,
Wang KaiTuo,
Zhang HongYin,
Li LanFen
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111011377
Subject(s) - argininosuccinate lyase , escherichia coli , streptococcus mutans , crystallization , recombinant dna , lyase , arginine , chemistry , bacteria , gene , enzyme , biology , microbiology and biotechnology , biochemistry , crystallography , amino acid , genetics , urea cycle , organic chemistry
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 ( sm ASL) was amplified and cloned into expression vector pET28a. The recombinant sm ASL 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 R 3, with unit‐cell parameters a = b = 254.5, c = 78.3 Å.
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