Crystallization and preliminary X-ray diffraction analysis of GCIP/HHM transcriptional regulator
Crystallization and preliminary X-ray diffraction analysis of GCIP/HHM transcriptional regulator
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DOI：
10.1107/s1744309108038219
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发表时间：
2009-01-01
影响因子：
0.9
通讯作者：
Nureki, Osamu
中科院分区：
文献类型：
--
作者：
Seto, Azusa;Ikushima, Hiroaki;Nureki, Osamu
GCIP/HHM 是一种人核蛋白，参与细胞增殖的调节。其一级结构包含螺旋-环-螺旋和亮氨酸-拉链基序，但缺乏DNA结合基本区域。使用悬滴蒸气扩散法获得全长 GCIP/HHM 的天然和硒代蛋氨酸衍生 (SeMet) 晶体。通过添加三(2-羧乙基)膦作为还原剂，晶体得到了极大的改善，衍射分辨率达到3.5埃。使用从 SeMet 晶体获得的数据集进行的初步相计算表明，该晶体属于空间群 P3(2)21，并且每个不对称单元包含一个分子。使用 SeMet 晶体通过多波长反常色散法进行结构测定正在进行中。
GCIP/HHM is a human nuclear protein that is implicated in regulation of cell proliferation. Its primary structure contains helix-loop-helix and leucine-zipper motifs but lacks a DNA-binding basic region. Native and selenomethionine-derivatized (SeMet) crystals of full-length GCIP/HHM were obtained using the hanging-drop vapour-diffusion method. The crystals were greatly improved by adding tris(2-carboxyethyl)phosphine as a reducing reagent and diffracted to 3.5 angstrom resolution. Preliminary phase calculations using the data set obtained from the SeMet crystal suggested that the crystal belonged to space group P3(2)21 and contained one molecule per asymmetric unit. Structure determination by the multiple-wavelength anomalous dispersion method using the SeMet crystals is in progress.