人瓣状核酸内切酶1催化结构域与带切口的DNA产物复合物的结晶及初步晶体学分析：使用DPCS试剂盒实现高效的蛋白质-DNA复合物结晶
Crystallization and preliminary crystallographic analysis of the catalytic domain of human flap endonuclease 1 in complex with a nicked DNA product: use of a DPCS kit for efficient protein-DNA complex crystallization.
作者信息
Sakurai Shigeru, Kitano Ken, Morioka Hiroshi, Hakoshima Toshio
机构信息
Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jan 1;64(Pt 1):39-43. doi: 10.1107/S1744309107065372. Epub 2007 Dec 20.
Abstract
Flap endonuclease 1 (FEN1) is a structure-specific nuclease that removes the RNA/DNA primer associated with Okazaki fragments in DNA replication. Here, crystals of the complex between the catalytic domain of human FEN1 and a DNA product have been obtained. For efficient crystallization screening, a DNA-protein complex crystallization screening (DPCS) kit was designed based on commercial crystallization kits. The crystal was found to belong to space group P2(1), with unit-cell parameters a = 61.0, b = 101.3, c = 106.4 A, beta = 106.4 degrees. The asymmetric unit is predicted to contain two complexes in the crystallographic asymmetric unit. A diffraction data set was collected to a resolution of 2.75 A.
摘要
瓣内切核酸酶1（FEN1）是一种结构特异性核酸酶，可去除DNA复制过程中与冈崎片段相关的RNA/DNA引物。在此，已获得人FEN1催化结构域与DNA产物之间复合物的晶体。为了进行高效的结晶筛选，基于商业结晶试剂盒设计了一种DNA-蛋白质复合物结晶筛选（DPCS）试剂盒。发现该晶体属于空间群P2(1)，晶胞参数为a = 61.0、b = 101.3、c = 106.4 Å，β = 106.4°。预计不对称单位在晶体学不对称单位中包含两个复合物。收集了分辨率为2.75 Å的衍射数据集。
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