Fujishima A, Hakoshima T, Tomita K
Biotechnology Laboratories, Takeda Chemical Industries Ltd., Osaka, Japan.
J Mol Biol. 1987 Sep 20;197(2):373-4. doi: 10.1016/0022-2836(87)90131-8.
Recombinant human interleukin 2 produced by Escherichia coli was purified to homogeneity and crystallized after being separated from methionyl interleukin 2. Crystals suitable for structural studies have been obtained by the seed enlargement technique, using the method of vapor diffusion with ammonium sulfate as the precipitant at pH 4.6. The space group is P2(1)2(1)2 with cell dimensions a = 49.2 A, b = 87.6 A and c = 32.4 A. The asymmetric unit contains one molecule of the protein. From preliminary results, the crystals are moderately stable to X-rays and produce measurable reflections to a resolution of about 2.2 A. The diffraction data for the native crystals have been collected on a diffractometer at 2.4 A resolution.
通过大肠杆菌产生的重组人白细胞介素2在与甲硫氨酰白细胞介素2分离后被纯化至同质并结晶。采用种子放大技术，以硫酸铵为沉淀剂，在pH 4.6条件下通过气相扩散法获得了适合进行结构研究的晶体。空间群为P2(1)2(1)2，晶胞参数a = 49.2 Å，b = 87.6 Å，c = 32.4 Å。不对称单元包含一个蛋白质分子。根据初步结果，这些晶体对X射线具有一定稳定性，能产生分辨率约为2.2 Å的可测量反射。已在衍射仪上以2.4 Å分辨率收集了天然晶体的衍射数据。
