PRELIMINARY INVESTIGATION OF CRYSTALS OF THE NEUTRAL LIPASE FROM PSEUDOMONAS-FLUORESCENS

被引：15

作者：

LARSON, S

DAY, J

GREENWOOD, A

OLIVER, J

RUBINGH, D

MCPHERSON, A

机构：

[1] UNIV CALIF RIVERSIDE,DEPT BIOCHEM,RIVERSIDE,CA 92521

[2] PROCTER & GAMBLE CO,MIAMI VALLEY LABS,CINCINNATI,OH 45247

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1991年 / 222卷 / 01期

关键词：

LIPASE; X-RAY DIFFRACTION; PROTEIN CRYSTALS;

D O I：

10.1016/0022-2836(91)90732-L

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：

The neutral lipase from the bacteria Pseudomonas fluorescens, marketed under the trade name LpL-200S, has been crystallized in a form suitable for X-ray diffraction analysis from 35% n-propanol at pH 8·5. The crystals are monoclinic prisms and are of space group C2 with a = 91·00 A ̊, b = 47·17 A ̊, c = 35·21 A ̊ and β = 121·43 °. There is one molecule of the protein as the asymmetric unit of the crystals. The diffraction pattern extends to at least 1·6 Å resolution and the crystals are extremely robust in terms of X-ray exposure. © 1991.

引用

页码：21 / 22

页数：2

共 7 条

[1] A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTER OF A TRIACYLGLYCEROL LIPASE [J].