Bacchella L, Lina C, Todone F, Negri A, Tedeschi G, Ronchi S, Mattevi A
Dipartimento di Genetica e Microbiologia, Università di Pavia, Via Abbiategrasso 207, 27100 Pavia, Italy.
Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):549-51. doi: 10.1107/s0907444998011913.
The flavoenzyme L-aspartate oxidase from Escherichia coli was crystallized using the hanging-drop vapour-diffusion technique with PEG 4000 as precipitant. The crystals belong to space group P3121 (or P3221) with unit-cell parameters a = b = 84.9, c = 159.9 A. A solvent content of 42% corresponds to a monomer (60 kDa) in the asymmetric unit. A complete 2.8 A resolution data set was collected using a rotating-anode X-ray generator.
利用悬滴气相扩散技术，以聚乙二醇4000作为沉淀剂，使来自大肠杆菌的黄素酶L-天冬氨酸氧化酶结晶。晶体属于空间群P3121（或P3221），晶胞参数a = b = 84.9，c = 159.9 Å。42%的溶剂含量对应于不对称单元中的一个单体（60 kDa）。使用旋转阳极X射线发生器收集了完整的2.8 Å分辨率数据集。
