PRELIMINARY INVESTIGATION OF CRYSTALS OF LIPASE-I FROM RHIZOPUS-NIVEUS

被引：7

作者：

KOHNO, M

KUGIMIYA, W

HASHIMOTO, Y

MORITA, Y

机构：

[1] Central Research Institute, Tsukuba R and D Center, Fuji Oil Co., Ltd., Tsukuba-Gun, Ibaraki 300-24, 4-3 Kinunodai, Yaicara

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 229卷 / 03期

关键词：

LIPASE; PROTEIN CRYSTALS; RHIZOPUS-NIVEUS; STRUCTURE; X-RAY DIFFRACTION;

D O I：

10.1006/jmbi.1993.1080

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：

Lipase I from Rhizopus niveus consists of two polypeptide chains bound non-covalently. Lipase I has been crystallized in a form suitable for X-ray diffraction analysis using the hanging drop method of vapour diffusion at 20°C. The crystals grew at pH 6.0 to 7.0 using 14 to 16% polyethylene glycol 8000 as the precipitant. The crystals are tetragonal with space group P41 (or P43) and cell dimensions of a = b = 83.7 Å, c = 137.9 Å. There are two protein molecules in the asymmetric unit. The diffraction pattern extends to at least 2.5 Å resolution. © 1993 Academic Press, Inc.

引用

页码：785 / 786

页数：2

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