Purification, crystallization and preliminary X-ray diffraction of a complex between IL-10 and soluble IL-10R1

被引：21

作者：

Josephson, K

McPherson, DT

Walter, MR ^{[1
]}

机构：

[1] Univ Alabama Birmingham, Ctr Biophys Sci & Engn, Birmingham, AL 35294 USA

[2] Univ Alabama Birmingham, Dept Microbiol, Birmingham, AL 35294 USA

[3] Univ Alabama Birmingham, Ctr AIDS Res, Birmingham, AL 35294 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444901016249

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A complex between interleukin-10 and the extracellular domain of its high-affinity receptor (sIL-10R1) has been crystallized from polyethylene glycol solutions. Crystals suitable for diffraction analysis required the modification of the NXS/T glycosylation sites on sIL-10R1 by site-directed mutagenesis and inclusion of the detergent cyclohexyl-methyl-beta -D-maltopyranoside in the crystallization experiments. The crystals belong to space group P3(2)12 or its enantimorph P3(1)12, with unit-cell parameters a=b=46.23, c=307.78 Angstrom, alpha=beta =90, gamma =120 degrees, and diffract X-rays to similar to2.9 Angstrom. The IL-10 dimer is positioned on a crystallographic twofold, resulting in one IL-10 chain and one sIL-10R1 chain in the asymmetric unit, which corresponds to a solvent content of approximately 44%.

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页码：1908 / 1911

页数：4

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