Hwang Heejin, Kim Sungsoo, Park Sohyun, Ngo Tri Duc, Kim Kyeong Kyu, Kim T Doohun
Department of Molecular Science and Technology, Graduate School of Interdisciplinary Programs, Ajou University, Suwon 443-749, Republic of Korea.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):572-4. doi: 10.1107/S1744309111007706. Epub 2011 Apr 27.
Industrial demand for active biocatalysts with desirable biochemical properties is constantly increasing and the discovery and characterization of novel esterases is potentially useful for industrial processes. Here, X-ray crystallographic studies of an (R)-specific SGNH arylesterase (Sm23) from Sinorhizobium meliloti 1021 are reported. The recombinant protein was expressed in Escherichia coli with a His tag and purified to homogeneity. Sm23 was crystallized using 0.2 M magnesium formate as a precipitant and X-ray diffraction data were collected to a resolution of 2.2 Å with an R(merge) of 6.9%. The crystals of SM23 belonged to the I-centred tetragonal space group I4(1)22, with unit-cell parameters a = b = 126.6, c = 190.9 Å. A molecular-replacement solution was obtained using the crystal structure of arylesterase from Mycobacterium smegmatis as a template.
工业界对具有理想生化特性的活性生物催化剂的需求不断增加，新型酯酶的发现和表征对工业过程可能具有重要意义。在此，我们报道了来自苜蓿中华根瘤菌1021的一种（R）特异性SGNH芳基酯酶（Sm23）的X射线晶体学研究。重组蛋白在大肠杆菌中表达，带有His标签，并纯化至同质。Sm23以0.2 M甲酸镁作为沉淀剂进行结晶，收集到分辨率为2.2 Å、R(merge)为6.9%的X射线衍射数据。Sm23的晶体属于I中心四方空间群I4(1)22，晶胞参数a = b = 126.6，c = 190.9 Å。以耻垢分枝杆菌芳基酯酶的晶体结构为模板，获得了分子置换解。
