大肠杆菌肽基 - tRNA水解酶的结晶及初步X射线分析
Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase.
作者信息
Schmitt E, Fromant M, Plateau P, Mechulam Y, Blanquet S
机构信息
Laboratoire de Biochimie, Unité de Recherche Associée 1970 du Centre National de la Recherche Scientifique, Palaiseau, France.
出版信息
Proteins. 1997 May;28(1):135-6. doi: 10.1002/(sici)1097-0134(199705)28:1<135::aid-prot14>3.0.co;2-k.
Peptidyl-tRNA hydrolase from Escherichia coli, a monomer of 21 kDa, was overexpressed from its cloned gene pth and crystallized by using polyethylene glycol as precipitant. The crystals are orthorhombic and have unit cell parameters a = 47.24 A, b = 63.59 A, and c = 62.57 A. They belong to space group P2(1)2(1)2(1) and diffract to better than 1.2 A resolution. The structure is being solved by multiple isomorphous replacement.
来自大肠杆菌的肽基 - tRNA水解酶，是一种21 kDa的单体，通过其克隆基因pth进行过表达，并使用聚乙二醇作为沉淀剂进行结晶。晶体为正交晶系，晶胞参数a = 47.24 Å，b = 63.59 Å，c = 62.57 Å。它们属于空间群P2(1)2(1)2(1)，衍射分辨率优于1.2 Å。该结构正在通过多同晶置换法解析。
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