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Crystallization and preliminary X-ray crystallographic studies of recombinant human leukotriene A4 hydrolase complexed with bestatin.

作者信息

Tsuge H, Ago H, Aoki M, Furuno M, Noma M, Miyano M, Minami M, Izumi T, Shimizu T

机构信息

Life Science Research Laboratory, Japan Tobacco, Inc., Kanagawa.

出版信息

J Mol Biol. 1994 May 20;238(5):854-6. doi: 10.1006/jmbi.1994.1341.

Abstract

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 I2(1)2(1)2(1) with unit cell dimensions of a = 273.6 A, b = 261.3 A and c = 52.9 A. They diffract beyond 2.5 A resolution and a native data set up to 3 A resolution has been collected on an imaging plate Weissenberg camera using synchrotron radiation.

摘要

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