Lin Long Liu, Merlino Antonello
Department of Applied Chemistry, National Chiayi University, 300 Syuefu Road, Chiayi City 60004, Taiwan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):669-72. doi: 10.1107/S1744309113012165. Epub 2013 May 25.
Here, the crystallization and preliminary X-ray diffraction studies of Bacillus licheniformis γ-glutamyl transpeptidase (BlGT) are reported. The serendipitous finding of heterogeneous nucleants in the initial experiments provided the first crystallization conditions for the protein. Crystals were grown by hanging-drop vapour diffusion using a precipitant solution consisting of 20%(w/v) PEG 3350, 0.2 M magnesium chloride hexahydrate, 0.1 M Tris-HCl pH 8.2. The protein crystallized in the orthorhombic space group P2(1)2(1)2(1), with one heterodimer per asymmetric unit and unit-cell parameters a = 60.90, b = 61.97, c = 148.24 Å. The BlGT crystals diffracted to 2.95 Å resolution.
本文报道了地衣芽孢杆菌γ-谷氨酰转肽酶(BlGT)的结晶及初步X射线衍射研究。在初始实验中意外发现的异质成核剂为该蛋白提供了首个结晶条件。采用由20%(w/v)聚乙二醇3350、0.2 M六水合氯化镁、0.1 M Tris-HCl(pH 8.2)组成的沉淀剂溶液,通过悬滴气相扩散法生长晶体。该蛋白在正交晶系空间群P2(1)2(1)2(1)中结晶,每个不对称单元有一个异二聚体,晶胞参数a = 60.90、b = 61.97、c = 148.24 Å。BlGT晶体的衍射分辨率达到2.95 Å。