Hassell A M, Johanson K O, Goodhart P, Young P R, Holskin B P, Carr S A, Roberts G D, Simon P L, Chen M J, Lewis M
Department of Macromolecular Sciences, Smith Kline & French Laboratories, King of Prussia, Pennsylvania 19406.
J Biol Chem. 1989 Mar 25;264(9):4948-52.
Human interleukin-1 alpha, cloned and expressed in E. coli, has been purified and structurally characterized by various physiochemical methods, including mass spectrometry. The recombinant protein has been crystallized by the hanging drop vapor diffusion method using dimethyl sulfoxide as the precipitating agent. The space group is P2(1)2(1)2(1). Unit cell dimensions are a = 44.1, b = 57.1, and c = 61.7 A and alpha = beta = gamma = 90 degrees. The crystals diffract to beyond 1.7 A and are suitable for high resolution data collection. Native diffraction data were collected. Screens for heavy atom derivatives have been initiated.
在大肠杆菌中克隆并表达的人白细胞介素-1α，已通过包括质谱分析在内的各种物理化学方法进行了纯化和结构表征。该重组蛋白已通过悬滴气相扩散法，以二甲基亚砜作为沉淀剂进行了结晶。空间群为P2(1)2(1)2(1)。晶胞参数为a = 44.1，b = 57.1，c = 61.7 Å，α = β = γ = 90°。这些晶体的衍射分辨率超过1.7 Å，适合进行高分辨率数据收集。已收集了天然衍射数据。已开始进行重原子衍生物筛选。
