重组人白细胞介素-5的结晶及初步X射线衍射研究

Crystallization and preliminary X-ray diffraction studies of recombinant human interleukin-5.

作者信息

Hassell A M, Wells T N, Graber P, Proudfoot A E, Anderegg R J, Burkhart W, Jordan S R, Milburn M V

机构信息

Glaxo Research Institute, Department of Structural and Biophysical Chemistry, Research Triangle Park, NC 27709.

出版信息

J Mol Biol. 1993 Feb 20;229(4):1150-2. doi: 10.1006/jmbi.1993.1110.

DOI:10.1006/jmbi.1993.1110

PMID:8445640

Abstract

Recombinant human interleukin-5 (rhIL-5) has been crystallized by the hanging drop vapor diffusion method using 0.1 M-Tris.HCl buffer (pH 8.5) containing 0.2 to 0.25 M-sodium acetate and 26 to 30% PEG 4000 at 22 degrees C. The parallel-piped crystals belong to the space group C2 with unit cell dimensions of a = 122.1 A, b = 36.11 A, c = 56.42 A, beta = 98.59 degrees. They diffract to at least 2.0 A resolution on a rotating anode X-ray source. The molecular mass weight of the protein and the volume of the unit cell suggest that the asymmetric unit contains one intermolecular disulfide-bonded homodimer.

摘要

重组人白细胞介素-5（rhIL-5）已通过悬滴气相扩散法在22℃下结晶，所用缓冲液为含0.2至0.25 M醋酸钠和26至30%聚乙二醇4000的0.1 M - Tris.HCl缓冲液（pH 8.5）。平行六面体晶体属于空间群C2，晶胞参数为a = 122.1 Å，b = 36.11 Å，c = 56.42 Å，β = 98.59°。在旋转阳极X射线源上，它们的衍射分辨率至少为2.0 Å。蛋白质的分子量和晶胞体积表明不对称单元包含一个分子间二硫键连接的同型二聚体。