PURIFICATION, FUNCTIONAL-CHARACTERIZATION, AND CRYSTALLIZATION OF THE LIGAND-BINDING DOMAIN OF THE RETINOID-X RECEPTOR
PURIFICATION, FUNCTIONAL-CHARACTERIZATION, AND CRYSTALLIZATION OF THE LIGAND-BINDING DOMAIN OF THE RETINOID-X RECEPTOR
复制标题
DOI：
10.1006/prep.1995.1079
复制
发表时间：
1995-10-01
影响因子：
1.6
通讯作者：
GRONEMEYER, H
中科院分区：
文献类型：
--
作者：
BOURGUET, W;RUFF, M;GRONEMEYER, H
人类视黄酸X受体α (hRXR α)的配体结合域（LED）在大肠杆菌中过量产生，纯化纯度超过95%，功能均匀。RXR α - LBD的圆二色性光谱表明，该蛋白主要由螺旋结构和螺旋结构组成，在含100 mM管（pH 7.0）和1.5柠檬酸铵的储层中，采用蒸汽扩散法生长晶体。它们属于六角形空间群P6(3)22，单元胞参数a = b = 110.8埃，c = 109.9埃，α = β = 90度，γ = 120度，使用同步辐射衍射X射线，分辨率极限为2.5埃。晶体的不对称单元包含一个分子，溶剂含量约为55%，V-m值为3.6埃/道尔顿。(C) 1995学术出版社，Inc。
The ligand binding domain (LED) of the human retinoid X receptor alpha (hRXR alpha) was overproduced in Escherichia coli and purified to more than 95% purity and functional homogeneity. Circular dichroism spectra of the purified RXR alpha LBD indicated that the protein was composed predominantly of cy-helical structures and coils, Crystals were grown from ammonium citrate using the vapor diffusion method against st reservoir containing 100 mM Pipes (pH 7.0) and 1.5 as ammonium citrate. They belong to the hexagonal space group P6(3)22 with unit cell parameters a = b = 110.8 Angstrom and c = 109.9 Angstrom, alpha = beta = 90 degrees, gamma = 120 degrees, and they diffract X rays to a resolution limit of 2.5 Angstrom using synchrotron radiation. The asymmetric unit of the crystals contains one molecule with a solvent content of approximately 55% and a V-m value of 3.6 Angstrom(3)/dalton. (C) 1995 Academic Press, Inc.