Crystallization and preliminary X-ray crystallographic analysis of DFPase from Loligo vulgaris

被引:16
作者
Scharff, EI
Lücke, C
Fritzsch, G
Koepke, J
Hartleib, J
Dierl, S
Rüterjans, H
机构
[1] Univ Frankfurt, Inst Biophys Chem, D-60439 Frankfurt, Germany
[2] Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60528 Frankfurt, Germany
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷
关键词
D O I
10.1107/S0907444900014232
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
'Squid-type' diisopropylfluorophosphatases (DFPases), a subclass of the phosphotriesterases, are enzymes capable of hydrolysing organophosphorus nerve agents. To date, no three-dimensional structure of a 'squid-type' DFPase is known. Here, the crystallization of the DFPase originally isolated from head ganglion of the squid Loligo vulgaris is reported. The protein has been heterologously expressed in Escherichia coli, purified to homogeneity and subsequently crystallized. The protein crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 43.1, b = 82.1, c = 86.6 Angstrom and one monomer per asymmetric unit. Under cryoconditions (120 K) the crystals diffracted beyond 2.0 Angstrom using a Cu rotating-anode X-ray generator.
引用
收藏
页码:148 / 149
页数:2
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