CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF RECOMBINANT HUMAN INTERLEUKIN-5

被引：8

作者：

HASSELL, AM ^{[1
]}

WELLS, TNC ^{[1
]}

GRABER, P ^{[1
]}

PROUDFOOT, AEI ^{[1
]}

ANDEREGG, RJ ^{[1
]}

BURKHART, W ^{[1
]}

JORDAN, SR ^{[1
]}

MILBURN, MV ^{[1
]}

机构：

[1] GLAXO INST MOLEC BIOL,CH-1228 PLAN LES OUATES,SWITZERLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 229卷 / 04期

关键词：

INTERLEUKIN-5; EOSINOPHIL DIFFERENTIATION FACTOR; CRYSTALLIZATION; EOSINOPHIL; CYTOKINE;

D O I：

10.1006/jmbi.1993.1110

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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°C. The parallelepiped crystals belong to the space group C2 with unit cell dimensions of a = 122.1 Å, b = 36.11 Å, c = 56.42 Å, β = 98.59°. They diffract to at least 2.0 Å 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. © 1993 Academic Press, Inc.

引用

页码：1150 / 1152

页数：3

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