变构分支酸变位酶的结晶及初步X射线分析
The crystallization and preliminary X-ray analysis of allosteric chorismate mutase.
作者信息
Xue Y, Lipscomb W N
机构信息
Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.
出版信息
J Mol Biol. 1994 Aug 12;241(2):273-4. doi: 10.1006/jmbi.1994.1497.
An allosteric chorismate mutase, the Thr226-->Ile mutant, from the yeast Saccharomyces cerevisiae has been crystallized in space group P6(1)(P6(5)) using the hanging drop vapour diffusion method at room temperature. The cell dimensions are a = b = 95.8 A, c = 157.9 A, alpha = beta = 90 degrees, gamma = 120 degrees. It contains a dimer in the crystallographic asymmetric unit. The crystal diffracts to 2.2 A resolution. A native data set has been collected to 82% completeness at this resolution.
来自酿酒酵母的一种变构分支酸变位酶，即苏氨酸226突变为异亮氨酸的突变体，已采用悬滴气相扩散法在室温下结晶于空间群P6(1)(P6(5))中。晶胞参数为a = b = 95.8 Å，c = 157.9 Å，α = β = 90°，γ = 120°。其晶体学不对称单元中包含一个二聚体。该晶体的衍射分辨率达到2.2 Å。已在该分辨率下收集到完整度为82%的天然数据集。
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