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本文引用的文献

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Crystal structures of two aminoglycoside kinases bound with a eukaryotic protein kinase inhibitor.两种氨基糖苷激酶与真核蛋白激酶抑制剂结合的晶体结构。
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CR8, a potent and selective, roscovitine-derived inhibitor of cyclin-dependent kinases.CR8，一种强效且具选择性的、源自罗斯考维汀的细胞周期蛋白依赖性激酶抑制剂。
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对SAD-1激酶结构域的初步晶体学分析，SAD-1是秀丽隐杆线虫突触前分化所必需的一种蛋白质。

Preliminary crystallographic analysis of the kinase domain of SAD-1, a protein essential for presynaptic differentiation in Caenorhabditis elegans.

作者信息

Yan Xiaojie, Shen Yuequan

机构信息

Department of BMB, Basic Medical College, Tianjin Medical University, Tianjin 300070, People's Republic of China.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):449-52. doi: 10.1107/S1744309113006088. Epub 2013 Mar 28.

DOI:10.1107/S1744309113006088
PMID:23545657
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3614176/
Abstract

SAD-1 is a serine/threonine kinase which plays an important role in the regulation of both neuronal polarity and synapse formation in Caenorhabditis elegans. The kinase domain of SAD-1 from C. elegans was overexpressed in Escherichia coli BL21 (DE3) cells and purified to homogeneity using nickel-nitrilotriacetic acid metal-affinity, ion-exchange and gel-filtration chromatography. Diffraction-quality crystals were grown using the sitting-drop vapour-diffusion technique from a condition consisting of 1 M CAPSO pH 9.6, 10%(w/v) polyethylene glycol 3350. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 205.4, b = 57.1, c = 71.7 Å, β = 106.1°. X-ray diffraction data were recorded to 3.0 Å resolution from a single crystal using synchrotron radiation.

摘要

SAD-1是一种丝氨酸/苏氨酸激酶，在秀丽隐杆线虫的神经元极性和突触形成调节中发挥重要作用。来自秀丽隐杆线虫的SAD-1激酶结构域在大肠杆菌BL21(DE3)细胞中过表达，并使用镍-次氮基三乙酸金属亲和、离子交换和凝胶过滤色谱法纯化至同质。使用坐滴气相扩散技术，从由1 M CAPSO pH 9.6、10%（w/v）聚乙二醇3350组成的条件中生长出衍射质量的晶体。这些晶体属于单斜空间群C2，晶胞参数为a = 205.4、b = 57.1、c = 71.7 Å，β = 106.1°。使用同步辐射从单晶记录了分辨率为3.0 Å的X射线衍射数据。