与过渡态类似物复合的分支酸变位酶催化抗体的结晶及初步结构研究。
Crystallization and preliminary structural studies of a chorismate mutase catalytic antibody complexed with a transition state analog.
作者信息
Haynes M R, Stura E A, Hilvert D, Wilson I A
机构信息
Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037.
出版信息
Proteins. 1994 Feb;18(2):198-200. doi: 10.1002/prot.340180211.
The Fab' fragment of a catalytic antibody with chorismate mutase activity has been crystallized as a complex with the transition-state analog hapten. The complex was crystallized by the vapor diffusion method using ammonium sulfate as the precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a = 37.1 A, b = 63.3 A, c = 178.5 A, and there is one Fab' molecule per asymmetric unit. The crystals diffract X-rays to at least 3.0 A and are suitable for X-ray crystallographic studies.
具有分支酸变位酶活性的催化抗体的Fab'片段已与过渡态类似物半抗原形成复合物结晶。该复合物通过气相扩散法，以硫酸铵作为沉淀剂进行结晶。晶体属于正交晶系空间群P2(1)2(1)2(1)，晶胞参数a = 37.1 Å，b = 63.3 Å，c = 178.5 Å，每个不对称单元中有一个Fab'分子。这些晶体对X射线的衍射分辨率至少达到3.0 Å，适合进行X射线晶体学研究。
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