Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans
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Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans. / Cao, Yan Li; Li, Gui Lan; Wang, Kai Tuo; Zhang, Hong Yin; Li, Lan Fen.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, No. 6, 01.06.2011, p. 682-684.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans
AU - Cao, Yan Li
AU - Li, Gui Lan
AU - Wang, Kai Tuo
AU - Zhang, Hong Yin
AU - Li, Lan Fen
PY - 2011/6/1
Y1 - 2011/6/1
N2 - 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.
AB - 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.
KW - argininosuccinate lyase
KW - Streptococcus mutans
UR - http://www.scopus.com/inward/record.url?scp=79958101763&partnerID=8YFLogxK
U2 - 10.1107/S1744309111011377
DO - 10.1107/S1744309111011377
M3 - Journal article
C2 - 21636911
AN - SCOPUS:79958101763
VL - 67
SP - 682
EP - 684
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
SN - 2053-230X
IS - 6
ER -
ID: 234874408