Cloning, expression, purification and preliminary X-ray crystallographic studies of 2-methylisocitrate lyase from Salmonella typhimurium

被引：2
|
作者：
Simanshu, DK
Satheshkumar, PS
Parthasarathy, S
Savithri, HS
Murthy, MRN [1 ]
机构：
[1] Indian Inst Sci, Mol Biophys Unit, Bangalore 560012, Karnataka, India
[2] Indian Inst Sci, Dept Biochem, Bangalore 560012, Karnataka, India
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷
关键词：
D O I：
10.1107/S0907444902015858
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
In Salmonella typhimurium, propionate is oxidized to pyruvate via the 2-methylcitric acid cycle. The last step of this cycle, the cleavage of 2-methylisocitrate to succinate and pyruvate, is catalysed by 2-methylisocitrate lyase (EC 4.1.3.30). Methylisocitrate lyase (molecular weight 32 kDa) with a C-terminal polyhistidine affinity tag has been cloned and overexpressed in Escherichia coli and purified and crystallized under different conditions using the hanging-drop vapour-diffusion technique. Crystals belong to the orthogonal space group P2(1)2(1)2(1), with unit-cell parameters a = 63.600, b = 100.670, c = 204.745 Angstrom. A complete data set to 2.5 Angstrom resolution has been collected using an image-plate detector system mounted on a rotating-anode X-ray generator.
引用
收藏
页码：2159 / 2161
页数：3
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