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

页码：854 / 856

页数：3

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