人肝脏α-烯醇化酶的结晶及X射线初步分析
Crystallization and preliminary X-ray analysis of human liver alpha-enolase.
作者信息
Wang Juan, Zhou Yan Feng, Li Lan Fen, Su Xiao Dong
机构信息
Peking University, Beijing, People's Republic of China.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt 3):288-90. doi: 10.1107/S1744309109004138. Epub 2009 Feb 26.
Abstract
Enolase is a multifunctional enzyme that plays important roles in many biological and disease processes. alpha-Enolase from human liver (hENO1) was expressed as a soluble protein and purified by affinity column chromatography and gel filtration. Crystals were obtained by the hanging-drop vapour-diffusion method and diffracted to 2.5 A resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 72.85, b = 66.02, c = 79.43 A, beta = 94.54 degrees .
摘要
烯醇化酶是一种多功能酶，在许多生物学和疾病过程中发挥重要作用。人肝脏中的α-烯醇化酶（hENO1）以可溶性蛋白形式表达，并通过亲和柱色谱法和凝胶过滤法进行纯化。通过悬滴气相扩散法获得晶体，并衍射至2.5埃分辨率。晶体属于空间群P2(1)，晶胞参数为a = 72.85，b = 66.02，c = 79.43埃，β = 94.54°。
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