Carrasco-López César, Godoy Cesar, de las Rivas Blanca, Fernández-Lorente Gloria, Palomo José M, Guisán José M, Fernández-Lafuente Roberto, Martínez-Ripoll Martín, Hermoso Juan A
Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto de Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):1043-5. doi: 10.1107/S1744309108031928. Epub 2008 Oct 31.
Bacillus thermocatenulatus lipase 2 (BTL2) is a thermoalkalophilic lipase that has been reported as an enantioselective biocatalyst for diverse reactions and that heads a group of enzymes that share high resistance towards many inactivation agents (heat, organic solvents, pH etc.). This makes BTL2 an important research target because of its potential industrial applications. BTL2 was cloned and overexpressed in Escherichia coli, purified and concentrated for crystallization using the sitting-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 13% MPD and 0.2 M ammonium acetate in 0.05 M sodium citrate pH 5.5-5.6. The crystals, which belonged to the orthorhombic space group I222 with unit-cell parameters a = 73.07, b = 129.08, c = 127.49 A, allowed the collection of an X-ray data set to 2.2 A resolution.
嗜热链状芽孢杆菌脂肪酶2（BTL2）是一种嗜热嗜碱脂肪酶，据报道它是多种反应的对映选择性生物催化剂，并且是一组对许多失活剂（热、有机溶剂、pH等）具有高抗性的酶中的一种。由于其潜在的工业应用，这使得BTL2成为一个重要的研究目标。BTL2在大肠杆菌中克隆并过量表达，经纯化和浓缩后，于291 K使用坐滴气相扩散法进行结晶。晶体从含有13% 2-甲基-2,4-戊二醇和0.2 M醋酸铵的0.05 M柠檬酸钠pH 5.5 - 5.6的混合物中生长。这些晶体属于正交晶系空间群I222，晶胞参数a = 73.07，b = 129.08，c = 127.49 Å，能够收集到分辨率为2.2 Å的X射线数据集。
