Purification, crystallization and preliminary X-ray analysis of a Nup107-Nup133 heterodimeric nucleoporin complex.
Purification, crystallization and preliminary X-ray analysis of a Nup107-Nup133 heterodimeric nucleoporin complex.
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Nup107-Nup133 异二聚核孔蛋白复合物的纯化、结晶和初步 X 射线分析。
DOI:
10.1107/s1744309107040523
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发表时间:
2007
期刊:
影响因子:
--
通讯作者:
Schwartz,ThomasU
中科院分区:
文献类型:
--
作者:
Boehmer,Thomas;Schwartz,ThomasU
The nuclear pore complex (NPC), the sole gateway of traffic between the nucleus and the cytoplasm, is built up from multiple copies of about 30 proteins collectively termed nucleoporins (nups). Nups are organized into distinct subcomplexes. Nup107 and Nup133 are members of the essential Nup107–160 subcomplex, a component of the central NPC architecture. A dimeric complex of the C-terminal domains of human Nup107 and Nup133 was expressed from a bicistronic vector in Escherichia coli, purified and crystallized in two different crystal forms. Crystals grown in the presence of 18–22% PEG 3350 belong to space group P212121 and diffracted to 2.9 Å. Native and seleno-l-methionine-derivative crystals grown in the presence of 1.1 M sodium malonate belong to space group C2 and diffracted to 2.55 and 2.9 Å, respectively. Structure determination of this complex will give the first insights into the protein–protein interactions within a core module of the NPC.
影响因子:
3.3
作者:
Orjalo, Arturo V.;Arnaoutov, Alexei;Forbes, Douglass J.
通讯作者:
Forbes, Douglass J.
影响因子:
16
作者:
Harel, A;Orjalo, AV;Forbes, DJ
通讯作者:
Forbes, DJ