CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT HUMAN LEUKOTRIENE A(4) HYDROLASE COMPLEXED WITH BESTATIN

被引：16
|
作者：
TSUGE, H [1 ]
AGO, H [1 ]
AOKI, M [1 ]
FURUNO, M [1 ]
NOMA, M [1 ]
MIYANO, M [1 ]
MINAMI, M [1 ]
IZUMI, T [1 ]
SHIMIZU, T [1 ]
机构：
[1] UNIV TOKYO,FAC MED,DEPT BIOCHEM,BUNKYO KU,TOKYO 113,JAPAN
来源：
JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 238卷 / 05期
关键词：
LEUKOTRIENE A(4) HYDROLASE; BESTATIN; CRYSTALLIZATION; ZINC-METALLOPROTEASE; AMINOPEPTIDASE;
D O I：
10.1006/jmbi.1994.1341
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 leukotriene A4 hydrolase complexed with bestatin, an inhibitor of metalloprotease, has been crystallized by the hanging drop vapor diffusion method using 0·1 M phosphate buffer (pH 6·5) and 50 to 54% saturated ammonium sulfate. The orthorhombic crystals belong to the space group I222 or I212121 with unit cell dimensions of a = 273·6 Å, b = 261·3Å and c = 52·9 Å. They diffract beyond 2·5 Å resolution and a native data set up to 3 Å resolution has been collected on an imaging plate Weissenberg camera using synchrotron radiation. © 1994, Academic Press Limited.
引用
收藏
页码：854 / 856
页数：3
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