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启动对II类果糖-1,6-二磷酸醛缩酶的晶体学研究。

Initiating a crystallographic study of a class II fructose-1,6-bisphosphate aldolase.

作者信息

Naismith J H, Ferrara J D, Bailey S, Marshall K, Dauter Z, Wilson K S, Habash J, Harrop S J, Berry A J, Hunter W N

机构信息

Department of Chemistry, University of Manchester, U.K.

出版信息

J Mol Biol. 1992 Jun 20;225(4):1137-41. doi: 10.1016/0022-2836(92)90113-x.

DOI:10.1016/0022-2836(92)90113-x
PMID:1613797
Abstract

We have reproducibly crystallized the metal-dependent Class II fructose-1,6-bisphosphate aldolase from Escherichia coli. Crystals in the shape of truncated hexagonal bipyramids have unit cell dimensions of a = b = 78.4 A, c = 290.6 A and are suitable for a detailed structural analysis. The space group has been identified as P6(1)22 or enantiomorph. Data sets to approximately 2.9 A resolution have been recorded using both the Rigaku R-AXIS IIc image plate area detector coupled to a copper target rotating anode X-ray source and using the MAR image plate systems with synchrotron radiation at the EMBL outstation DESY in Hamburg, and at S.R.S. Daresbury. Diffraction beyond 2.5 A has been observed when large freshly grown crystals are used with the synchrotron beam. A data set to this resolution has been collected. Several putative heavy-atom derivative data sets have also been measured using synchrotron radiation facilities and analysis of these data sets is in progress.

摘要

我们已成功重复结晶出大肠杆菌中依赖金属的Ⅱ类果糖-1,6-二磷酸醛缩酶。截顶六方双锥体形状的晶体,其晶胞参数为a = b = 78.4 Å,c = 290.6 Å,适合进行详细的结构分析。已确定空间群为P6(1)22或对映体。使用与铜靶旋转阳极X射线源耦合的理学R-AXIS IIc成像板面积探测器,以及在汉堡的欧洲分子生物学实验室分站DESY和达累斯伯里的同步辐射源使用MAR成像板系统,记录了分辨率约为2.9 Å的数据集。当使用大型新生长的晶体与同步辐射光束时,观察到了超过2.5 Å的衍射。已收集到该分辨率的数据集。还使用同步辐射设施测量了几个推定的重原子衍生物数据集,对这些数据集的分析正在进行中。

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