Wright Helena, Barona-Gómez Francisco, Hodgson David A, Fülöp Vilmos
Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, England.
Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):534-6. doi: 10.1107/S0907444903028877. Epub 2004 Feb 25.
The priA gene encoding the enzyme phosphoribosyl isomerase from Streptomyces coelicolor, a novel bifunctional enzyme involved in both histidine and tryptophan biosynthesis, was heterologously expressed and purified in Escherichia coli as an N-terminal His-tag fusion. The purified recombinant enzyme was crystallized using the hanging-drop method in 1.50 M ammonium sulfate and 100 mM sodium citrate pH 4.8. Crystals were obtained of up to 0.05 x 0.05 x 0.3 mm in size. A full data set to 2 A resolution was collected at the ESRF beamline ID14-1 and space group P3(1,2)21 was assigned, with unit-cell parameters a = 65.1, c = 104.7 A.
来自天蓝色链霉菌的编码磷酸核糖异构酶的priA基因，是一种参与组氨酸和色氨酸生物合成的新型双功能酶，在大肠杆菌中作为N端His标签融合蛋白进行了异源表达和纯化。使用悬滴法在1.50 M硫酸铵和pH 4.8的100 mM柠檬酸钠中对纯化的重组酶进行结晶。获得了尺寸达0.05×0.05×0.3 mm的晶体。在欧洲同步辐射装置（ESRF）的ID14-1光束线上收集了分辨率为2 Å的完整数据集，并确定其空间群为P3(1,2)21，晶胞参数a = 65.1，c = 104.7 Å。
