Overproduction, crystallization and preliminary X-ray crystallographic analysis of Escherichia coli tRNA N6-threonylcarbamoyladenosine dehydratase

被引:3
|
作者
Kim, Sunmin [1 ]
Kim, Keon Young [1 ]
Park, Jeong Kuk [1 ]
Lee, Byung Il [2 ]
Kim, Yun-Gon [3 ]
Park, SangYoun [1 ]
机构
[1] Soongsil Univ, Sch Syst Biomed Sci, Seoul 156743, South Korea
[2] Natl Canc Ctr, Res Inst, Div Convergence Technol, Biomol Funct Res Branch, Goyang 410769, Gyeonggi, South Korea
[3] Soongsil Univ, Dept Chem Engn, Seoul 156743, South Korea
关键词
PROTEIN; ACID;
D O I
10.1107/S2053230X14020883
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Escherichia coli tRNA N-6-threonylcarbamoyladenosine dehydratase (TcdA), previously called CsdL or YgdL, was overproduced and purified from E. coli and crystallized using polyethylene glycol 3350 as a crystallizing agent. X-ray diffraction data were collected to 2.70 angstrom resolution under cryoconditions using synchrotron X-rays. The crystals belonged to space group P2(1), with unit-cell parameters a = 65.4, b = 96.8, c = 83.3 angstrom, beta = 111.7 degrees. According to the Matthews coefficient, the asymmetric unit may contain up to four subunits of the monomeric protein, with a crystal volume per protein mass (V-M) of 2.12 angstrom(3) Da(-1) and 42.1% solvent content.
引用
收藏
页码:1517 / 1520
页数:4
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