Crystallization and preliminary crystallographic study of a recombinant phospholipase D from cowpea (Vigna unguiculata L. Walp)

被引：6

作者：

Abergel, C

Abousalham, A

Chenivesse, S

Rivière, M

Moustacas-Gardies, AM

Verger, R

机构：

[1] AVENTIS, CNRS, UMR 1889, F-13402 Marseille 20, France

[2] Lab Lipolyse Enzymat, CNRS, UPR 9025, F-13402 Marseille, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444900020825

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The plant phospholipase D (PLD) is considered to be a key enzyme involved in various physiological processes such as signal transduction and membrane metabolism. Crystals of the PLD protein from Vigna unguiculata have been produced from the recombinant 768 amino-acid protein. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 157.7, b = 65.6, c = 90.2 Angstrom, beta = 111.5 degrees. There is one molecule in the asymmetric unit. Frozen crystals diffract to at least 1.94 Angstrom resolution using synchrotron radiation. A search for heavy-atom derivatives using ytterbium and tungstate is currently under way in order to solve the three-dimensional structure.

引用

页码：320 / 322

页数：3

共 34 条

[1] Study of fatty acid specificity of sunflower phospholipase D using detergent/phospholipid micelles [J].