酵母核小体组装因子Cia1p的纯化、结晶及初步X射线衍射分析
Purification, crystallization and preliminary X-ray diffraction analysis of yeast nucleosome-assembly factor Cia1p.
作者信息
Padmanabhan Balasundaram, Kataoka Kazuhiro, Adachi Naruhiko, Horikoshi Masami
机构信息
Horikoshi Gene Selector Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation (JST), 5-9-6 Tokodai, Tsukuba, Ibaraki 300-2635, Japan.
出版信息
Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 2):1876-8. doi: 10.1107/s0907444902013860. Epub 2002 Sep 28.
Yeast Cia1p is a homologue of human CIA (CCG1-interacting factor A), which possesses nucleosome-assembly activity and interacts with the human TFIID subunit CCG1 and the C-terminal domain of histone H3. The yeast Cia1p without the C-terminal polyanionic stretch has been expressed in Escherichia coli, purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method using PEG 8000 as precipitant. The protein was crystallized in orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 106.70, b = 46.92, c = 40.60 A and one molecule in the asymmetric unit. The crystal diffracted beyond 2.95 A resolution using synchrotron radiation.
酵母Cia1p是人类CIA（CCG1相互作用因子A）的同源物，它具有核小体组装活性，并与人类TFIID亚基CCG1以及组蛋白H3的C末端结构域相互作用。不含C末端聚阴离子延伸的酵母Cia1p已在大肠杆菌中表达，纯化至同质，并使用PEG 8000作为沉淀剂通过悬滴气相扩散法结晶。该蛋白质在正交空间群P2(1)2(1)2(1)中结晶，晶胞参数a = 106.70，b = 46.92，c = 40.60 Å，不对称单元中有一个分子。使用同步辐射，该晶体的衍射分辨率超过2.95 Å。
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