中文摘要：

生物体β-化循环是脂肪酸氧化分解的主要途径，许多代谢疾病都与其密切相关。线虫β-化循环与人类相似，但与其相关的研究报道却很少。线虫基因C32E8．9编码的蛋白被WormBase命名为烯脂酰CoA水合酶（WormBase ID：CE29693），被推测具有催化β-化循环第二步反应的功能。作者将C32E8．9基因克隆到原核表达载体上，在大肠杆菌中获得高效表达，并分别纯化了母体蛋白以及硒代蛋白衍生物。多角度静态光散射实验表明该蛋白的聚合状态为三聚体。该蛋白在沉淀剂2-甲基-2，4-戊二醇的作用下形成可供衍射分析的六棱柱形状晶体，空间群为P21，晶胞参数为a=79．0A^°，b=82．4A^°，c=9．2A^°，α=γ=90．0°，β=120°，数据分析表明该晶体非单晶，是一种罕见的蛋白质“三晶”——包含三套晶格。

英文摘要：

The β-oxidation spiral is the main pathway of fatty acid degradation in mammalian cells and many metabolic diseases are related to the disorders of the β-oxidation spiral. The β-oxidation spiral of Caenorhabditis elegans （C.elegans） is similar to human but is rarely reported. The protein encoded by C.elegans C32E8.9 gene is named as enoyl-CoA hydratase （cECH） in WormBase （ID： CE29693）, which is considered to catalyze the second step of the β-oxidation spiral in C.elegans. C32E8.9 gene was cloned into a prokaryotic expression vector pEXS-DH. Recombinant cECH and its selenium derivative （Se-cECH） were expressed and purified intensively with high purity, cECH was found to form hexamer according to size exclusion chromatography with multi-angle light scattering detection. Both cECH and Se-cECH were successfully crystallized by using the precipitant, 2-Methyl-2, 4-pentanediol. The crystal belongs to space group P21 with unit cell a=79.0A^°, b=82.4A^°, c=79.2A^°, α=γ=90.0°,β=120°.Data analysis indicated that the crystal was not a monocrystal but an unusual tricrystal that contains three sets of lattices.